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

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 pathw...

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Published inFEBS letters Vol. 594; no. 23; pp. 3767 - 3775
Main Authors Thomas, Christoph, Aller, Stephen G., Beis, Konstantinos, Carpenter, Elisabeth P., Chang, Geoffrey, Chen, Lei, Dassa, Elie, Dean, Michael, Duong Van Hoa, Franck, Ekiert, Damian, Ford, Robert, Gaudet, Rachelle, Gong, Xin, Holland, I. Barry, Huang, Yihua, Kahne, Daniel K., Kato, Hiroaki, Koronakis, Vassilis, Koth, Christopher M., Lee, Youngsook, Lewinson, Oded, Lill, Roland, Martinoia, Enrico, Murakami, Satoshi, Pinkett, Heather W., Poolman, Bert, Rosenbaum, Daniel, Sarkadi, Balazs, Schmitt, Lutz, Schneider, Erwin, Shi, Yigong, Shyng, Show‐Ling, Slotboom, Dirk J., Tajkhorshid, Emad, Tieleman, D. Peter, Ueda, Kazumitsu, Váradi, András, Wen, Po‐Chao, Yan, Nieng, Zhang, Peng, Zheng, Hongjin, Zimmer, Jochen, Tampé, Robert
Format Journal Article
LanguageEnglish
Published England Wiley 01.12.2020
Subjects
ABC transporters
ATPases
cryo‐EM
evolution
functional diversity
Life Sciences
membrane proteins
molecular machines
phylogeny
primary active transporters
sequence alignment
structural biology
X‐ray crystallography
X-ray crystallography
primary active transporters
membrane proteins
sequence alignment
molecular machines
phylogeny
ABC transporters
structural biology
ATPases
cryo-EM
ABC Transporters
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Summary: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.
Bibliography:Edited by Gergely Szakács
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PMCID: PMC8386196
CT and RT wrote the manuscript with contributions from all coauthors. This review is the quintessence of a resumed discussion that started at the FEBS Advanced Lecture Course on the Biochemistry of Membrane Proteins in Budapest (2019) and continued at the FEBS Conference on ATP-Binding Cassette (ABC) Proteins in Innsbruck (2020). The discussion included a vivid exchange of thoughts via hundreds of emails and remote video sessions during the global COVID-19 pandemic. In addition to the authors listed, we received positive feedbacks on our proposed classification from several further leading scientists in the ABC transporter field. Yet, as they felt that their contribution was too small, they decided not to accept authorship.
Author contributions
ISSN:0014-5793
1873-3468
1873-3468
DOI:10.1002/1873-3468.13935