Structural and functional diversity calls for a new classification of ABC transporters

Christoph Thomas, Stephen G. Aller, Konstantinos Beis, Elisabeth P. Carpenter, Geoffrey Chang, Lei Chen, Elie Dassa, Michael Dean, Franck Duong Van Hoa, Damian Ekiert, Robert Ford, Rachelle Gaudet, Xin Gong, I. Barry Holland, Yihua Huang, Daniel K. Kahne, Hiroaki Kato, Vassilis Koronakis, Christopher M. Koth, Youngsook LeeOded Lewinson, Roland Lill, Enrico Martinoia, Satoshi Murakami, Heather W. Pinkett, Bert Poolman, Daniel Rosenbaum, Balazs Sarkadi, Lutz Schmitt, Erwin Schneider, Yigong Shi, Show Ling Shyng, Dirk J. Slotboom, Emad Tajkhorshid, D. Peter Tieleman, Kazumitsu Ueda, András Váradi, Po Chao Wen, Nieng Yan, Peng Zhang, Hongjin Zheng, Jochen Zimmer, Robert Tampé

Research output: Contribution to journalArticlepeer-review

154 Scopus citations


Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.

Original languageEnglish (US)
Pages (from-to)3767-3775
Number of pages9
JournalFEBS Letters
Issue number23
StatePublished - Dec 2020

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology


  • ABC transporters
  • ATPases
  • X-ray crystallography
  • cryo-EM
  • membrane proteins
  • molecular machines
  • phylogeny
  • primary active transporters
  • sequence alignment
  • structural biology


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