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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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Volume 385, Issue 10


How do ABC transporters drive transport?

Chris Van Der Does
  • Institute of Biochemistry, Biozentrum Frankfurt, Johann Wolfgang Goethe-University, Marie-Curie-Str. 9, D-60439 Frankfurt/Main, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Robert Tampé
  • Institute of Biochemistry, Biozentrum Frankfurt, Johann Wolfgang Goethe-University, Marie-Curie-Str. 9, D-60439 Frankfurt/Main, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.121


Members of the ATP-binding cassette (ABC) superfamily are integral membrane proteins that hydrolyze ATP to drive transport. In the last two decades these proteins have been extensively characterized on a genetic and biochemical level, and in recent years high-resolution crystal structures of several nucleotide-binding domains and full-length transporters have extended our knowledge. Here we discuss the possible mechanisms of transport that have been derived from these crystal structures and the extensive available biochemical data.

Keywords: ATP-binding cassette proteins; membrane proteins; nucleotide-binding proteins; structure; transport ATPases; transport mechanism

About the article

Published Online: 2005-06-01

Published in Print: 2004-10-01

Citation Information: Biological Chemistry, Volume 385, Issue 10, Pages 927–933, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.121.

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