Ins and outs of major facilitator superfamily antiporters

Christopher J. Law, Peter C. Maloney, Da Neng Wang

Research output: Contribution to journalArticle

Abstract

The major facilitator superfamily (MFS) represents the largest group of secondary active membrane transporters, and its members transport a diverse range of substrates. Recent work shows that MFS antiporters, and perhaps all members of the MFS, share the same three-dimensional structure, consisting of two domains that surround a substrate translocation pore. The advent of crystal structures of three MFS antiporters sheds light on their fundamental mechanism; they operate via a single binding site, alternating-access mechanism that involves a rocker-switch type movement of the two halves of the protein. In the sn-glycerol-3-phosphate transporter (GlpT) from Escherichia coli, the substrate-binding site is formed by several charged residues and a histidine that can be protonated. Salt-bridge formation and breakage are involved in the conformational changes of the protein during transport. In this review, we attempt to give an account of a set of mechanistic principles that characterize all MFS antiporters.

Original languageEnglish (US)
Pages (from-to)289-305
Number of pages17
JournalAnnual Review of Microbiology
Volume62
DOIs
Publication statusPublished - 2008

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Keywords

  • EmrD
  • GlpT
  • OxlT
  • Rocker-switch mechanism
  • Secondary membrane transporter proteins
  • UhpT

ASJC Scopus subject areas

  • Microbiology

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