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

• Published in: FEBS 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
• Language: English
• 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

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...