Molecular Basis of Alternating Access Membrane Transport by the Sodium-Hydantoin Transporter Mhp1

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, co...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2010-04, Vol.328 (5977), p.470-473
Hauptverfasser:	Shimamura, Tatsuro, Weyand, Simone, Beckstein, Oliver, Rutherford, Nicholas G, Hadden, Jonathan M, Sharples, David, Sansom, Mark S.P, Iwata, So, Henderson, Peter J.F, Cameron, Alexander D
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinomycetales - chemistry Actinomycetales - metabolism Amino Acid Motifs Atoms Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biological and medical sciences Biological Transport Cell physiology Crystal structure Crystallography, X-Ray Fundamental and applied biological sciences. Psychology Grants Hydantoins - chemistry Hydantoins - metabolism Ion Transport Membrane and intracellular transports Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Membranes Microbacterium Models, Molecular Molecular and cellular biology Molecular biology Molecular dynamics Molecular Dynamics Simulation Molecules Porters Protein Conformation Protein Folding Protein Structure, Secondary Proteins RESEARCH ARTICLE Rigid structures Sodium Sodium - metabolism
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