期刊
FEBS LETTERS
卷 594, 期 23, 页码 3767-3775出版社
WILEY
DOI: 10.1002/1873-3468.13935
关键词
ABC transporters; ATPases; cryo‐ EM; membrane proteins; molecular machines; phylogeny; primary active transporters; sequence alignment; structural biology; X‐ ray crystallography
资金
- Medical Research Council [MR/N020103/1, MR/N000994/1]
- Intramural Program of the NIH
- Wellcome Trust [101828/Z/13/Z]
- German Research Foundation [LI 415/5, SFB 807, TA157/12-1]
- Canada Research Chairs program
- Wellcome Trust [101828/Z/13/Z] Funding Source: Wellcome Trust
- MRC [MR/N000994/1, MR/N020103/1] Funding Source: UKRI
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.
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