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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: closed (30 December 2022) | Viewed by 23322

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Prof. Dr. Giuseppe Zanotti

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Guest Editor

Department of Biomedical Sciences, University of Padua, 35131 Padova, Italy
Interests: structural biology; protein crystallography; cryo-electron microscopy; bacterial proteins; Helicobacter pylori; transport proteins
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Zhongzhou Chen

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Guest Editor

State Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, China
Interests: structural biology; cancers; epigenetics; demethylation; transcription regulation; viral polymerase; drug discovery
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Since the determination of the first 3D crystal structure of myoglobin in 1958, protein crystallography has developed into a quite mature structural biology technique, solving ~87% of structures deposited in the Protein Data Bank (PDB). Moreover, in the last few years, two events have revolutionized the field of structural biology: the “resolution revolution” of cryo-electron Microscopy (cryo-EM), which allows the visualization of single particles at a near-atomic resolution without the need of growing them in a crystalline form, and the recent development of AlphaFold 2, an AI system able to predict the 3D structure of a single protein with high reliability. This last event will strongly influence crystallography since that most of the future crystal structures will be solved using the molecular replacement technique. In parallel, new techniques/methods are emerging in crystallography, such as new crystal growing methods, more intense and focused X-ray beams, novel data collection methods, ultra-sensitive detectors, advanced computational algorithms, and new software.

It is easy to foresee that in the next few years, the application of these techniques will revolutionize our understanding of the molecular mechanisms of cell biology, with a wide impact spanning across biochemistry, life science, and medicine. The present Special Issue is aimed at summarizing frontier technologies and methodological advances in the field, as well as structures and functions of special proteins or protein complexes, to take stock of the present situation and to create a virtual forum for the future of Structural Biology.

Prof. Dr. Giuseppe Zanotti
Prof. Dr. Zhongzhou Chen
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

protein crystallography
structural biology
high-throughput crystallography
cryo-EM
NMR
radiation sources
X-ray detectors
structure determination
molecular mechanism
functions
drug discovery

Related Special Issue

Emerging Topics in Protein Crystallography in International Journal of Molecular Sciences (5 articles)

Published Papers (12 papers)

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Research

15 pages, 5393 KiB

Open AccessArticle

Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae

by Jiyeon Jang and Jeong Ho Chang

Int. J. Mol. Sci. 2023, 24(6), 5139; https://doi.org/10.3390/ijms24065139 - 7 Mar 2023

Viewed by 1303

Abstract

Phosphoserine aminotransferase (PSAT) is a pyridoxal 5′-phosphate-dependent enzyme involved in the second step of the phosphorylated pathway of serine biosynthesis. PSAT catalyzes the transamination of 3-phosphohydroxypyruvate to 3-phosphoserine using L-glutamate as the amino donor. Although structural studies of PSAT have been performed from archaea and humans, no structural information is available from fungi. Therefore, to elucidate the structural features of fungal PSAT, we determined the crystal structure of Saccharomyces cerevisiae PSAT (ScPSAT) at a resolution of 2.8 Å. The results demonstrated that the ScPSAT protein was dimeric in its crystal structure. Moreover, the gate-keeping loop of ScPSAT exhibited a conformation similar to that of other species. Several distinct structural features in the halide-binding and active sites of ScPSAT were compared with its homologs. Overall, this study contributes to our current understanding of PSAT by identifying the structural features of fungal PSAT for the first time. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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13 pages, 3189 KiB

Open AccessArticle

Structures of MPND Reveal the Molecular Recognition of Nucleosomes

by Meiting Yang, Xiaorong Li, Zizi Tian, Lulu Ma, Jun Ma, Yunlong Liu, Guohui Shang, Ailing Liang, Wei Wu and Zhongzhou Chen

Int. J. Mol. Sci. 2023, 24(4), 3368; https://doi.org/10.3390/ijms24043368 - 8 Feb 2023

Cited by 2 | Viewed by 1749

Abstract

Adenine N⁶ methylation in DNA (6mA) is a well-known epigenetic modification in bacteria, phages, and eukaryotes. Recent research has identified the Mpr1/Pad1 N-terminal (MPN) domain-containing protein (MPND) as a sensor protein that may recognize DNA 6mA modification in eukaryotes. However, the structural details of MPND and the molecular mechanism of their interaction remain unknown. Herein, we report the first crystal structures of the apo–MPND and MPND–DNA complex at resolutions of 2.06 Å and 2.47 Å, respectively. In solution, the assemblies of both apo–MPND and MPND–DNA are dynamic. In addition, MPND was found to possess the ability to bind directly to histones, no matter the N-terminal restriction enzyme-adenine methylase-associated domain or the C-terminal MPN domain. Moreover, the DNA and the two acidic regions of MPND synergistically enhance the interaction between MPND and histones. Therefore, our findings provide the first structural information regarding the MPND–DNA complex and also provide evidence of MPND–nucleosome interactions, thereby laying the foundation for further studies on gene control and transcriptional regulation. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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18 pages, 4592 KiB

Open AccessArticle

Activity and Crystal Structure of the Adherent-Invasive Escherichia coli Tle3/Tli3 T6SS Effector/Immunity Complex Determined Using an AlphaFold2 Predicted Model

by Thi Thu Hang Le, Christine Kellenberger, Marie Boyer, Pierre Santucci, Nicolas Flaugnatti, Eric Cascales, Alain Roussel, Stéphane Canaan, Laure Journet and Christian Cambillau

Int. J. Mol. Sci. 2023, 24(2), 1740; https://doi.org/10.3390/ijms24021740 - 16 Jan 2023

Cited by 2 | Viewed by 2641

Abstract

The type VI secretion system (T6SS) delivers enzymatic effectors into target cells to destroy them. Cells of the same strain protect themselves against effectors with immunity proteins that specifically inhibit effectors. Here, we report the identification and characterization of a Tle3 phospholipase effector and its cognate immunity protein Tli3—an outer membrane lipoprotein from adherent-invasive Escherichia coli (AIEC). Enzymatic assays demonstrate that purified Tle3^AIEC has a phospholipase A1, and not A2, activity and that its toxicity is neutralized by the cognate immunity protein Tli3^AIEC. Tli3^AIEC binds Tle3 in a 1:1 stoichiometric ratio. Tle3^AIEC, Tli3^AIEC and the Tle3^AIEC-Tli3^AIEC complex were purified and subjected to crystallization. The Tle3^AIEC-Tli3^AIEC complex structure could not be solved by SeMet phasing, but only by molecular replacement when using an AlphaFold2 prediction model. Tle3^AIEC exhibits an α/β-hydrolase fold decorated by two protruding segments, including a N-terminus loop. Tli3^AIEC displays a new fold of three stacked β-sheets and a protruding loop that inserts in Tle3^AIECcatalytic crevice. We showed, experimentally, that Tle3^AIEC interacts with the VgrG ^AIEC cargo protein and AlphaFold2 prediction of the VgrG^AIEC-Tle3^AIEC complex reveals a strong interaction between the VgrG^AIEC C-terminus adaptor and Tle3^AIEC N-terminal loop. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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12 pages, 8005 KiB

Open AccessArticle

Substrate Specificity of GSDA Revealed by Cocrystal Structures and Binding Studies

by Qian Jia, Jinbing Zhang, Hui Zeng, Jing Tang, Nan Xiao, Shangfang Gao, Huanxi Li and Wei Xie

Int. J. Mol. Sci. 2022, 23(23), 14976; https://doi.org/10.3390/ijms232314976 - 29 Nov 2022

Cited by 1 | Viewed by 1107

Abstract

In plants, guanosine deaminase (GSDA) catalyzes the deamination of guanosine for nitrogen recycling and re-utilization. We previously solved crystal structures of GSDA from Arabidopsis thaliana (AtGSDA) and identified several novel substrates for this enzyme, but the structural basis of the enzyme activation/inhibition is poorly understood. Here, we continued to solve 8 medium-to-high resolution (1.85–2.60 Å) cocrystal structures, which involved AtGSDA and its variants bound by a few ligands, and investigated their binding modes through structural studies and thermal shift analysis. Besides the lack of a 2-amino group of these guanosine derivatives, we discovered that AtGSDA’s inactivity was due to the its inability to seclude its active site. Furthermore, the C-termini of the enzyme displayed conformational diversities under certain circumstances. The lack of functional amino groups or poor interactions/geometries of the ligands at the active sites to meet the precise binding and activation requirements for deamination both contributed to AtGSDA’s inactivity toward the ligands. Altogether, our combined structural and biochemical studies provide insight into GSDA. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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15 pages, 674 KiB

Open AccessArticle

DNA Sequence and Structure under the Prism of Group Theory and Algebraic Surfaces

by Michel Planat, Marcelo M. Amaral, Fang Fang, David Chester, Raymond Aschheim and Klee Irwin

Int. J. Mol. Sci. 2022, 23(21), 13290; https://doi.org/10.3390/ijms232113290 - 31 Oct 2022

Cited by 1 | Viewed by 1971

Abstract

Taking a DNA sequence, a word with letters/bases A, T, G and C, as the relation between the generators of an infinite group

π

, one can discriminate between two important families: (i) the cardinality structure for conjugacy classes of subgroups of

π

[...] Read more.

Taking a DNA sequence, a word with letters/bases A, T, G and C, as the relation between the generators of an infinite group

π

, one can discriminate between two important families: (i) the cardinality structure for conjugacy classes of subgroups of

π

is that of a free group on one to four bases, and the DNA word, viewed as a substitution sequence, is aperiodic; (ii) the cardinality structure for conjugacy classes of subgroups of

π

is not that of a free group, the sequence is generally not aperiodic and topological properties of

π

have to be determined differently. The two cases rely on DNA conformations such as A-DNA, B-DNA, Z-DNA, G-quadruplexes, etc. We found a few salient results: Z-DNA, when involved in transcription, replication and regulation in a healthy situation, implies (i). The sequence of telomeric repeats comprising three distinct bases most of the time satisfies (i). For two-base sequences in the free case (i) or non-free case (ii), the topology of

π

may be found in terms of the

S L (2, C)

character variety of

π

and the attached algebraic surfaces. The linking of two unknotted curves—the Hopf link—may occur in the topology of

π

in cases of biological importance, in telomeres, G-quadruplexes, hairpins and junctions, a feature that we already found in the context of models of topological quantum computing. For three- and four-base sequences, other knotting configurations are noticed and a building block of the topology is the four-punctured sphere. Our methods have the potential to discriminate between potential diseases associated to the sequences. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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10 pages, 2283 KiB

Open AccessArticle

In Silico Structural Analysis of Serine Carboxypeptidase Nf314, a Potential Drug Target in Naegleria fowleri Infections

by Pablo A. Madero-Ayala, Rosa E. Mares-Alejandre and Marco A. Ramos-Ibarra

Int. J. Mol. Sci. 2022, 23(20), 12203; https://doi.org/10.3390/ijms232012203 - 13 Oct 2022

Cited by 2 | Viewed by 1957

Abstract

Naegleria fowleri, also known as the “brain-eating” amoeba, is a free-living protozoan that resides in freshwater bodies. This pathogenic amoeba infects humans as a casual event when swimming in contaminated water. Upon inhalation, N. fowleri invades the central nervous system and causes primary amoebic meningoencephalitis (PAM), a rapidly progressive and often fatal disease. Although PAM is considered rare, reducing its case fatality rate compels the search for pathogen-specific proteins with a structure–function relationship that favors their application as targets for discovering new or improved drugs against N. fowleri infections. Herein, we report a computational approach to study the structural features of Nf314 (a serine carboxypeptidase that is a virulence-related protein in N. fowleri infections) and assess its potential as a drug target, using bioinformatics tools and in silico molecular docking experiments. Our findings suggest that Nf314 has a ligand binding site suitable for the structure-based design of specific inhibitors. This study represents a further step toward postulating a reliable therapeutic target to treat PAM with drugs specifically aimed at blocking the pathogen proliferation by inhibiting protein function. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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11 pages, 2005 KiB

Open AccessArticle

Toward Real Real-Space Refinement of Atomic Models

by Alexandre G. Urzhumtsev and Vladimir Y. Lunin

Int. J. Mol. Sci. 2022, 23(20), 12101; https://doi.org/10.3390/ijms232012101 - 11 Oct 2022

Cited by 3 | Viewed by 977

Abstract

High-quality atomic models providing structural information are the results of their refinement versus diffraction data (reciprocal-space refinement), or versus experimental or experimentally based maps (real-space refinement). A proper real-space refinement can be achieved by comparing such a map with a map calculated from the atomic model. Similar to density distributions, the maps of a limited and even inhomogeneous resolution can also be calculated as sums of terms, known as atomic images, which are three-dimensional peaky functions surrounded by Fourier ripples. These atomic images and, consequently, the maps for the respective models, can be expressed analytically as functions of coordinates, atomic displacement parameters, and the local resolution. This work discusses the practical feasibility of such calculation for the real-space refinement of macromolecular atomic models. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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22 pages, 6381 KiB

Open AccessArticle

A New Structural Model of Apolipoprotein B100 Based on Computational Modeling and Cross Linking

by Kianoush Jeiran, Scott M. Gordon, Denis O. Sviridov, Angel M. Aponte, Amanda Haymond, Grzegorz Piszczek, Diego Lucero, Edward B. Neufeld, Iosif I. Vaisman, Lance Liotta, Ancha Baranova and Alan T. Remaley

Int. J. Mol. Sci. 2022, 23(19), 11480; https://doi.org/10.3390/ijms231911480 - 29 Sep 2022

Cited by 4 | Viewed by 2914

Abstract

ApoB-100 is a member of a large lipid transfer protein superfamily and is one of the main apolipoproteins found on low-density lipoprotein (LDL) and very low-density lipoprotein (VLDL) particles. Despite its clinical significance for the development of cardiovascular disease, there is limited information on apoB-100 structure. We have developed a novel method based on the “divide and conquer” algorithm, using PSIPRED software, by dividing apoB-100 into five subunits and 11 domains. Models of each domain were prepared using I-TASSER, DEMO, RoseTTAFold, Phyre2, and MODELLER. Subsequently, we used disuccinimidyl sulfoxide (DSSO), a new mass spectrometry cleavable cross-linker, and the known position of disulfide bonds to experimentally validate each model. We obtained 65 unique DSSO cross-links, of which 87.5% were within a 26 Å threshold in the final model. We also evaluated the positions of cysteine residues involved in the eight known disulfide bonds in apoB-100, and each pair was measured within the expected 5.6 Å constraint. Finally, multiple domains were combined by applying constraints based on detected long-range DSSO cross-links to generate five subunits, which were subsequently merged to achieve an uninterrupted architecture for apoB-100 around a lipoprotein particle. Moreover, the dynamics of apoB-100 during particle size transitions was examined by comparing VLDL and LDL computational models and using experimental cross-linking data. In addition, the proposed model of receptor ligand binding of apoB-100 provides new insights into some of its functions. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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12 pages, 2327 KiB

Open AccessArticle

Structural Basis for the Binding of Allosteric Activators Leucine and ADP to Mammalian Glutamate Dehydrogenase

by Vasily A. Aleshin, Victoria I. Bunik, Eduardo M. Bruch and Marco Bellinzoni

Int. J. Mol. Sci. 2022, 23(19), 11306; https://doi.org/10.3390/ijms231911306 - 25 Sep 2022

Cited by 2 | Viewed by 1668

Abstract

Glutamate dehydrogenase (GDH) plays a key role in the metabolism of glutamate, an important compound at a cross-road of carbon and nitrogen metabolism and a relevant neurotransmitter. Despite being one of the first discovered allosteric enzymes, GDH still poses challenges for structural characterization of its allosteric sites. Only the structures with ADP, and at low (3.5 Å) resolution, are available for mammalian GDH complexes with allosteric activators. Here, we aim at deciphering a structural basis for the GDH allosteric activation using bovine GDH as a model. For the first time, we report a mammalian GDH structure in a ternary complex with the activators leucine and ADP, co-crystallized with potassium ion, resolved to 2.45 Å. An improved 2.4-angstrom resolution of the GDH complex with ADP is also presented. The ternary complex with leucine and ADP differs from the binary complex with ADP by the conformation of GDH C-terminus, involved in the leucine binding and subunit interactions. The potassium site, identified in this work, may mediate interactions between the leucine and ADP binding sites. Our data provide novel insights into the mechanisms of GDH activation by leucine and ADP, linked to the enzyme regulation by (de)acetylation. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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14 pages, 3901 KiB

Open AccessArticle

Structural Insights into the Binding Propensity of Human SHIP2 SH2 to Oncogenic CagA Isoforms from Helicobacter pylori

by Zi Wang, Yubao Shan, Ru Wang, Heng Zhou, Rui Hu, Ying Li, Jiang Zhu, Yunhuang Yang and Maili Liu

Int. J. Mol. Sci. 2022, 23(19), 11299; https://doi.org/10.3390/ijms231911299 - 25 Sep 2022

Cited by 1 | Viewed by 1544

Abstract

SHIP2 is a multi-domain inositol 5-phosphatase binding to a variety of phosphotyrosine (pY)-containing proteins through its SH2 domain, so as to regulate various cell signaling pathways by modulating the phosphatidylinositol level in the plasma membrane. Unfavorably, Helicobacter pylori can hijack SHIP2 through the CagA protein to induce gastric cell carcinogenesis. To date, the interaction between SHIP2 and CagA was not analyzed from a structural point of view. Here, the binding of SHIP2-SH2 with Tyr-phosphorylated peptides from four EPIYA motifs (A/B/C/D) in CagA was studied using NMR spectroscopy. The results showed that EPIYA-C and -D bind to a similar interface of SHIP2-SH2, including a pY-binding pocket and a hydrophobic pocket, to achieve high affinity, while EPIYA-A and -B bind to a smaller interface of SHIP2-SH2 with weak affinity. By summarizing the interface and affinity of SHIP2-SH2 for CagA EPIYA-A/B/C/D, c-MET and FcgR2B ITIM, it was proposed that, potentially, SHIP2-SH2 has a selective preference for L > I > V for the aliphatic residues at the pY+3 position in its ligand. This study reveals the rule of the ligand sequence bound by SHIP2-SH2 and the mechanism by which CagA protein hijacks SHIP2, which will help design a peptide inhibitor against SHIP2-SH2. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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17 pages, 7615 KiB

Open AccessArticle

In Silico Molecular Dynamics of Griseofulvin and Its Derivatives Revealed Potential Therapeutic Applications for COVID-19

by Parisa Aris, Masoud Mohamadzadeh, Yulong Wei and Xuhua Xia

Int. J. Mol. Sci. 2022, 23(13), 6889; https://doi.org/10.3390/ijms23136889 - 21 Jun 2022

Cited by 5 | Viewed by 2441

Abstract

Treatment options for Coronavirus Disease 2019 (COVID-19) remain limited, and the option of repurposing approved drugs with promising medicinal properties is of increasing interest in therapeutic approaches to COVID-19. Using computational approaches, we examined griseofulvin and its derivatives against four key anti-SARS-CoV-2 targets: main protease, RdRp, spike protein receptor-binding domain (RBD), and human host angiotensin-converting enzyme 2 (ACE2). Molecular docking analysis revealed that griseofulvin (CID 441140) has the highest docking score (–6.8 kcal/mol) with main protease of SARS-CoV-2. Moreover, griseofulvin derivative M9 (CID 144564153) proved the most potent inhibitor with −9.49 kcal/mol, followed by A3 (CID 46844082) with −8.44 kcal/mol against M protease and ACE2, respectively. Additionally, H bond analysis revealed that compound A3 formed the highest number of hydrogen bonds, indicating the strongest inhibitory efficacy against ACE2. Further, molecular dynamics (MD) simulation analysis revealed that griseofulvin and these derivatives are structurally stable. These findings suggest that griseofulvin and its derivatives may be considered when designing future therapeutic options for SARS-CoV-2 infection. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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11 pages, 14176 KiB

Open AccessArticle

Structural Insights into the Ligand-Binding and -Releasing Mechanism of Helicoverpa armigera Pheromone-Binding Protein PBP1

by Jiangge Zheng, Meiting Yang, Kun Dong, Jianbo Zhang, Huali Wang, Mengjia Xie, Wei Wu, Yong-Jun Zhang and Zhongzhou Chen

Int. J. Mol. Sci. 2022, 23(3), 1190; https://doi.org/10.3390/ijms23031190 - 21 Jan 2022

Cited by 7 | Viewed by 1572

Abstract

Cotton bollworm (Helicoverpa armigera) is a worldwide agricultural pest in which the transport of pheromones is indispensable and perceived by pheromone-binding proteins (PBPs). However, three-dimensional structure, pheromone binding, and releasing mechanisms of PBPs are not completely illustrated. Here, we solved three structures of the cotton bollworm HarmPBP1 at different pH values and its complex with ligand, Z-9-hexadecenal. Although apo-HarmPBP1 adopts a common PBP scaffold of six α-helices surrounding a predominantly hydrophobic central pocket, the conformation is greatly distinct from other apo-PBPs. The Z-9-hexadecenal is bound mainly by hydrophobic interaction. The pheromone can enter this cavity through an opening between the helices α5 and α6, as well as the loop between α3 and α4. Structural analysis suggests that ligand entry into the pocket is followed by a shift of Lys94 and Lys138, which may act as a lid at the opening of the pocket. Acidic pH will cause a subtle structural change of the lid, which in turn affects its ligand-binding ability, differently from other family proteins. Taken together, this study provides structural bases for the interactions between pheromones and PBPs, the pH-induced conformational switch, and the design of small inhibitors to control cotton bollworms by disrupting male–female chemosensory communication. Full article

(This article belongs to the Special Issue Emerging Topics in Structural Biology)

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