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Molecular Basis of Alternating Access Membrane Transport by the Sodium-Hydantoin Transporter Mhp1
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Shimamura, Tatsuro, Weyand, Simone, Beckstein, Oliver, Rutherford, N. G., Hadden, J. M., Sharples, D., Sansom, M. S. P. (Mark S. P.), Iwata, So, Henderson, P. J. F. (Peter J. F.) and Cameron, Alexander (2010) Molecular Basis of Alternating Access Membrane Transport by the Sodium-Hydantoin Transporter Mhp1. Science, Vol. 328 (No. 5977). pp. 470-473. doi:10.1126/science.1186303 ISSN 0036-8075.
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Official URL: http://dx.doi.org/10.1126/science.1186303
Abstract
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.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Science | ||||
Publisher: | American Association for the Advancement of Science | ||||
ISSN: | 0036-8075 | ||||
Official Date: | 2010 | ||||
Dates: |
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Volume: | Vol. 328 | ||||
Number: | No. 5977 | ||||
Page Range: | pp. 470-473 | ||||
DOI: | 10.1126/science.1186303 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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