Effect of A22 on the Conformation of Bacterial Actin MreB
Abstract
:1. Introduction
2. Results and Discussion
2.1. A22 Impedes ATP-Induced Backbone Conformational Change in MreB
2.2. MreB Adopts One Main Low-Energy Structure in the Apo, ATP+, and ATP-A22+ States
2.3. The ATP-A22+ MreB Structure Differs from the ATP+ Form
2.4. A22 Affects the Conformational Change of the Ile55-Ile219 and Ser232-Val316 MreB Segments
2.5. Water Dynamics in the Active Site of MreB Protofilament
2.6. Proposed Effect of A22
3. Methods
3.1. Preparation of Structures
3.2. Molecular Dynamics Simulations
4. Conclusions
5. Recommendation
Supplementary Materials
Author Contributions
Funding
Conflicts of Interest
Abbreviations
PDB | Protein Data Bank |
CcMreB | Caulobacter cresentus MreB |
NT | Nucleotide |
MD | Molecular dynamics |
AMBER | Assisted Model Building and Energy Refinement |
GAFF | General Amber Force Field |
RMSD | Root Mean Square Deviation |
PCA | Principal Component Analysis |
FEL | Free Energy Landscape |
RMSF | Root Mean Square Fluctuation |
AMPPNP | Adenylyl imidodiphosphate |
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System | State of MreB Protofilament | ATP | A22 | Mg2+ | Time (ns) | Repeats |
---|---|---|---|---|---|---|
1 | Apo (no ATP and A22) | - | - | + | 100 | 3 |
2 | ATP-bound (ATP+) | + | - | + | 100 | 3 |
3 | ATP-A22-bound (ATP-A22+) | + | + | + | 100 | 3 |
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Awuni, E.; Mu, Y. Effect of A22 on the Conformation of Bacterial Actin MreB. Int. J. Mol. Sci. 2019, 20, 1304. https://doi.org/10.3390/ijms20061304
Awuni E, Mu Y. Effect of A22 on the Conformation of Bacterial Actin MreB. International Journal of Molecular Sciences. 2019; 20(6):1304. https://doi.org/10.3390/ijms20061304
Chicago/Turabian StyleAwuni, Elvis, and Yuguang Mu. 2019. "Effect of A22 on the Conformation of Bacterial Actin MreB" International Journal of Molecular Sciences 20, no. 6: 1304. https://doi.org/10.3390/ijms20061304