Mechanistic diversity in ATP-binding cassette (ABC) transporters

Nat Struct Mol Biol. 2016 Jun 7;23(6):487-93. doi: 10.1038/nsmb.3216.


ABC transporters catalyze transport reactions, such as the high-affinity uptake of micronutrients into bacteria and the export of cytotoxic compounds from mammalian cells. Crystal structures of ABC domains and full transporters have provided a framework for formulating reaction mechanisms of ATP-driven substrate transport, but recent studies have suggested remarkable mechanistic diversity within this protein family. This review evaluates the differing mechanistic proposals and outlines future directions for the exploration of ABC-transporter-catalyzed reactions.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / classification*
  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism
  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Bacteria / chemistry
  • Biological Transport
  • Catalytic Domain
  • Gene Expression
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Protein Binding
  • Protein Domains
  • Protein Folding
  • Protein Structure, Secondary


  • ATP-Binding Cassette Transporters
  • Adenosine Triphosphate