Christoph Thomas, Stephen G. Aller, Konstantinos Beis, Elisabeth P. Carpenter,
Geoffrey Chang, Lei Chen, Elie Dassa, Michel Dean, Franck Duong Van Hoa,
Damian Ekiert, Robert Ford, Rachelle Gaudet, Xin Gong, I. Barry Holland,
Yihua, Vassilis Koronakis, Christopher M. Koth, Youngsook Lee, Oded Lewinson,
Roland Lill, Enrico Martinoia, Satoshi Murakami, Heather W. Pinket, Bert
Poolman, Daniel Rosenbaum, Balazs Sarkadi, Lutz Schmitt, Erwin Schneider,
Yigong Shi, Show-Ling Shyng, Dirk J. Slotboom, Emad Tajkhorshid,
Kazumitsu Ueda D. Peter Tieleman, Andras Varadi, Po-Chao Wen, Nieng Yan, Peng
Zhang, Hongjin Zheng, Jochen Zimmer, and Robert Tampe.
Structural and functional diversity calls for a new classification of
ABC transporters.
FEBS Letters, 594:3767-3775, 2020.
THOM2020-ET
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 currently comprises
seven different types based on structural homology in the TMDs.
