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

TitleStructural and functional diversity calls for a new classification of ABC transporters.
Publication TypeJournal Article
Year of Publication2020
AuthorsThomas, C, Aller, SG, Beis, K, Carpenter, EP, Chang, G, Chen, L, Dassa, E, Dean, M, Van Hoa, FDuong, Ekiert, D, Ford, R, Gaudet, R, Gong, X, I Holland, B, Huang, Y, Kahne, DK, Kato, H, Koronakis, V, Koth, CM, Lee, Y, Lewinson, O, Lill, R, Martinoia, E, Murakami, S, Pinkett, HW, Poolman, B, Rosenbaum, D, Sarkadi, B, Schmitt, L, Schneider, E, Shi, Y, Shyng, S-L, Slotboom, DJ, Tajkhorshid, E, D Tieleman, P, Ueda, K, Váradi, A, Wen, P-C, Yan, N, Zhang, P, Zheng, H, Zimmer, J, Tampé, R
JournalFEBS Lett
Date Published2020 Sep 26
ISSN1873-3468
Abstract

<p>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.</p>

DOI10.1002/1873-3468.13935
Alternate JournalFEBS Lett
PubMed ID32978974
Grant List / / Canada Research Chairs /
/ / National Institute of Health /
MR/N000994/1 / MRC_ / Medical Research Council / United Kingdom
MR/N020103/1 / MRC_ / Medical Research Council / United Kingdom
101828/Z/13/Z / WT_ / Wellcome Trust / United Kingdom
LI 415/5 / / Deutsche Forschungsgemeinschaft /
SFB 807 / / Deutsche Forschungsgemeinschaft /
TA157/12-1 / / Deutsche Forschungsgemeinschaft /