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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.

Original publication

DOI

10.1126/science.1186303

Type

Journal article

Journal

Science

Publication Date

23/04/2010

Volume

328

Pages

470 - 473

Keywords

Actinomycetales, Amino Acid Motifs, Bacterial Proteins, Binding Sites, Biological Transport, Crystallography, X-Ray, Hydantoins, Ion Transport, Membrane Transport Proteins, Models, Molecular, Molecular Dynamics Simulation, Protein Conformation, Protein Folding, Protein Structure, Secondary, Sodium