Structural and functional diversity calls for a new classification of ABC transporters. Issue 23 (26th October 2020)

• Record Type: Journal Article
• 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;
• Is Part Of: FEBS letters. Volume 594:Issue 23(2020)
• Page Start: 3767
• Page End: 3775
• Publication Date: 2020-10-26
• Subjects: ABC transporters -- ATPases -- cryo‐EM -- membrane proteins -- molecular machines -- phylogeny -- primary active transporters -- sequence alignment -- structural biology -- X‐ray crystallography; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13935
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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.