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The alternating access mechanism of transport as observed in the sodium-hydantoin transporter Mhp1

DOI: 10.1107/S0909049510032449 DOI Help
PMID: 21169684 PMID Help

Authors: Simone Weyand (Imperial College London) , Tatsuro Shimamura (Imperial College, London; Kyoto University; Japan Science and Technology Agency) , Oliver Beckstein (University of Oxford) , Mark Sansom (University of Oxford) , So Iwata (Imperial College, Londo; Diamond Light Source; Japan Science and Technology Agency; Kyoto University; RIKEN) , Peter J. F. Henderson (University of Leeds) , Alexander Cameron (Imperial College, London; Japan Science and Technology Agency; Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Synchrotron Radiation , VOL 18 (1) , PAGES 20-23

State: Published (Approved)
Published: December 2010

Open Access Open Access

Abstract: Secondary active transporters move molecules across cell membranes by coupling this process to the energetically favourable downhill movement of ions or protons along an electrochemical gradient. They function by the alternating access model of transport in which, through conformational changes, the substrate binding site alternately faces either side of the membrane. Owing to the difficulties in obtaining the crystal structure of a single transporter in different conformational states, relatively little structural information is known to explain how this process occurs. Here, the structure of the sodium-benzylhydantoin transporter, Mhp1, from Microbacterium liquefaciens, has been determined in three conformational states; from this a mechanism is proposed for switching from the outward-facing open conformation through an occluded structure to the inward-facing open state.

Journal Keywords: Hydantoins; Membrane Transport; Molecular Biology; Molecular Structure

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
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Added On: 11/11/2010 13:47

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