TY - JOUR A1 - Thomas, Christoph A1 - Aller, Stephen G. A1 - Beis, Konstantinos A1 - Carpenter, Elisabeth P. A1 - Chang, Geoffrey A1 - Chen, Lei A1 - Dassa, Elie A1 - Dean, Michael A1 - Duong Van Hoa, Franck A1 - Ekiert, Damian A1 - Ford, Robert A1 - Gaudet, Rachelle A1 - Gong, Xin A1 - Holland, I. Barry A1 - Huang, Yihua A1 - Kahne, Daniel K. A1 - Kato, Hiroaki A1 - Koronakis, Vassilis A1 - Koth, Christopher M. A1 - Lee, Youngsook A1 - Lewinson, Oded A1 - Lill, Roland A1 - Martinoia, Enrico A1 - Murakami, Satoshi A1 - Pinkett, Heather W. A1 - Poolman, Bert A1 - Rosenbaum, Daniel A1 - Sarkadi, Balazs A1 - Schmitt, Lutz A1 - Schneider, Erwin A1 - Shi, Yigong A1 - Shyng, Show‐Ling A1 - Slotboom, Dirk Jan A1 - Tajkhorshid, Emad A1 - Tieleman, Dirk Peter A1 - Ueda, Kazumitsu A1 - Váradi, András A1 - Wen, Po‐Chao A1 - Yan, Nieng A1 - Zhang, Peng A1 - Zheng, Hongjin A1 - Zimmer, Jochen A1 - Tampé, Robert T1 - Structural and functional diversity calls for a new classification of ABC transporters T2 - FEBS Letters N2 - 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: KW - ABC transporters KW - ATPases KW - cryo-EM KW - membrane proteins KW - molecular machines KW - phylogeny KW - primary active transporters KW - sequence alignment KW - structural biology KW - X-ray crystallography Y1 - 2020 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/57017 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-570178 SN - 1873-3468 SN - 0014-5793 VL - 2020 PB - Wiley CY - Chichester ER -