Journal
SCIENCE
Volume 328, Issue 5977, Pages 470-473Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1186303
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/C51725]
- European Union [LSHG-CT-2004-504601, 201924]
- Wellcome Trust [062164/Z/00/Z]
- Leverhulme Trust
- European Molecular Biology Organization
- BBSRC MPSi [BBS/B/14418]
- S. Suzuki and Ajinomoto Company Incorporated
- Japan Science and Technology Agency
- MEXT, Japan
- [21370043]
- Biotechnology and Biological Sciences Research Council [BB/C51725X/1, BEP17032, BB/G020043/1, B19456, BB/G023425/1, BBS/B/16011, BB/H000267/1, BBS/B/14418] Funding Source: researchfish
- BBSRC [BB/G023425/1, BB/H000267/1, BB/G020043/1] Funding Source: UKRI
- Grants-in-Aid for Scientific Research [21370043] Funding Source: KAKEN
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The structure of the sodium-benzylhydantoin transport protein Mhp1 from Microbacterium liquefaciens comprises a five-helix inverted repeat, which is widespread among secondary transporters. Here, we report the crystal structure of an inward-facing conformation of Mhp1 at 3.8 angstroms resolution, complementing its previously described structures in outward-facing and occluded states. From analyses of the three structures and molecular dynamics simulations, we propose a mechanism for the transport cycle in Mhp1. Switching from the outward-to the inward-facing state, to effect the inward release of sodium and benzylhydantoin, is primarily achieved by a rigid body movement of transmembrane helices 3, 4, 8, and 9 relative to the rest of the protein. This forms the basis of an alternating access mechanism applicable to many transporters of this emerging superfamily.
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