Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism
Abstract
:1. Introduction
2. Results
2.1. Inward_Apo
- D162-R17—the interaction between D162 (TM 5) and R17 (TM 1) is present in 93.6% of the simulation time for the three replicas;
- D229-R371—the salt-bridge between the D229 (loop TM6-TM7) and R371 (TM 11) can be observed in 97.1% of the simulation time for the three replicas;
- D28-R284—the salt-bridge between D28 and R284, present for about 95.8% of the simulation time for the three replicas, is located in the upper TM region and stabilizes the interaction between the N (TM1) and C (TM8) domains;
- E10-K150—this salt bridge, present in 52.5% of the simulation time for the three replicas, connects the C-terminal end of TM1 with the N-terminal end of TM5;
- E277-H180—this interaction (present in about 62.8% of the simulation time for the three replicas) appears to be essential for establishing the interaction of L-TM5-TM6 with TM8, characterizing the inward-facing conformation.
2.2. Outward_Apo
2.3. Inward_Fe
3. Discussion
4. Materials and Methods
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
Abbreviations
MSF | Major Facilitator Superfamily |
MD | Molecular Dynamics |
hFpn | Human Ferroportin |
BdFpn | Bdellovibrio bacteriovorus Ferroportin |
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System | Duration (ns) | Conformational State | Iron | Number of Simulations |
---|---|---|---|---|
Inward_Apo | 200 | Inward-facing | - | 3 |
Outward_Apo | 200 | Outward-facing | - | 3 |
Inward_Fe | 200 | Inward-facing | + | 3 |
Residue | Occupancy |
---|---|
D24 | 18.2% |
D134 | 33.3% |
S130 | 18.3% |
E203 | 11.1% |
D229 | 13.8% |
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Tortosa, V.; Bonaccorsi di Patti, M.C.; Iacovelli, F.; Pasquadibisceglie, A.; Falconi, M.; Musci, G.; Polticelli, F. Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism. Int. J. Mol. Sci. 2020, 21, 6785. https://doi.org/10.3390/ijms21186785
Tortosa V, Bonaccorsi di Patti MC, Iacovelli F, Pasquadibisceglie A, Falconi M, Musci G, Polticelli F. Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism. International Journal of Molecular Sciences. 2020; 21(18):6785. https://doi.org/10.3390/ijms21186785
Chicago/Turabian StyleTortosa, Valentina, Maria Carmela Bonaccorsi di Patti, Federico Iacovelli, Andrea Pasquadibisceglie, Mattia Falconi, Giovanni Musci, and Fabio Polticelli. 2020. "Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism" International Journal of Molecular Sciences 21, no. 18: 6785. https://doi.org/10.3390/ijms21186785