Title | Structural and functional diversity calls for a new classification of ABC transporters. |
Publication Type | Journal Article |
Year of Publication | 2020 |
Authors | Thomas, 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 |
Journal | FEBS Lett |
Volume | 594 |
Issue | 23 |
Pagination | 3767-3775 |
Date Published | 2020 Dec |
ISSN | 1873-3468 |
Keywords | ATP-Binding Cassette Transporters, Protein Domains, Protein Folding |
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> |
DOI | 10.1002/1873-3468.13935 |
Alternate Journal | FEBS Lett |
PubMed ID | 32978974 |
PubMed Central ID | PMC8386196 |
Grant List | R01 GM140584 / GM / NIGMS NIH HHS / United States MR/N000994/1 / MRC_ / Medical Research Council / United Kingdom 101828/Z/13/Z / WT_ / Wellcome Trust / United Kingdom R01 GM126626 / GM / NIGMS NIH HHS / United States R01 DK066485 / DK / NIDDK NIH HHS / United States MR/N020103/1 / MRC_ / Medical Research Council / United Kingdom / WT_ / Wellcome Trust / United Kingdom |