ABC transporters: how small machines do a big job

Amy L. Davidson, Peter C. Maloney

Research output: Contribution to journalReview articlepeer-review

Abstract

Transporters from the ATP-binding cassette (ABC) superfamily operate in all organisms, from bacteria to humans, to pump substances across biological membranes. Recent high-resolution views of ABC transporters in different conformational states provide clues as to how ATP might be used to drive the structural reorganizations that accompany membrane transport. Importantly, it now appears that a putative translocation pathway running through the center of the transporter might be gated alternately, either at the inside or the outside of the cytoplasmic membrane, coupling substrate translocation to a cycle of ATP-dependent conformational changes. ATP binding and ATP hydrolysis have distinct roles in this cycle: binding favors the outward-facing orientation, whereas hydrolysis returns the transporter to an inward-facing conformation.

Original languageEnglish (US)
Pages (from-to)448-455
Number of pages8
JournalTrends in Microbiology
Volume15
Issue number10
DOIs
StatePublished - Oct 2007

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)
  • Infectious Diseases
  • Virology

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