Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1
| Autor: | Mark S.P. Sansom, Nicholas G. Rutherford, Simone Weyand, Jonathan M. Hadden, So Iwata, Peter J. F. Henderson, Oliver Beckstein, David Sharples, Alexander D. Cameron, Tatsuro Shimamura |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Protein Folding Stereochemistry Protein Conformation Amino Acid Motifs Molecular Dynamics Simulation Crystallography X-Ray Article Protein Structure Secondary 03 medical and health sciences Molecular dynamics 0302 clinical medicine Protein structure Bacterial Proteins Actinomycetales Ion transporter 030304 developmental biology 0303 health sciences Multidisciplinary Binding Sites Ion Transport biology Membrane transport protein Chemistry Hydantoins Sodium Membrane Transport Proteins Biological Transport Membrane transport 3. Good health Transport protein Transmembrane domain biology.protein Protein folding 030217 neurology & neurosurgery |
| Zdroj: | Science; Vol 328 |
| Popis: | Triangulating to Mechanism Cellular uptake and release of a variety of substrates are mediated by secondary transporters, but no crystal structures are known for all three fundamental states of the transport cycle, which has limited explanations for their proposed mechanisms. Shimamura et al. (p. 470 ) report a 3.8-angstrom structure of the inward-facing conformation of the bacterial sodium-benzylhydantoin transport protein, Mhp1, complementing the other two available structures. Molecular modeling for the interconversions of these structures shows a simple rigid body rotation of four helices relative to the rest of the structure in which the protein switches reversibly from outward- to inward-facing. |
| Databáze: | OpenAIRE |
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