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

Simone Weyand, Tatsuro Shimamura, Oliver Beckstein, Mark S.P. Sansom, So Iwata, Peter J.F. Henderson, Alexander D. Cameron

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)20-23
Number of pages4
JournalJournal of synchrotron radiation
Volume18
Issue number1
DOIs
StatePublished - Jan 2011

Keywords

  • alternating access
  • hydantoins
  • membrane transport
  • transport protein

ASJC Scopus subject areas

  • Radiation
  • Nuclear and High Energy Physics
  • Instrumentation

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