4.4 Article

Structural basis for the mechanism of ABC transporters

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 43, 期 -, 页码 889-893

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST20150047

关键词

ATP-binding cassette (ABC) exporter; ATP-binding cassette (ABC) importer; ATP-binding cassette (ABC) transporter mechanism; membrane protein structure

资金

  1. Biotechnology and Biological Sciences Research Council [BB/H01778X/1]
  2. BBSRC [BB/H01778X/1] Funding Source: UKRI
  3. Biotechnology and Biological Sciences Research Council [BB/H01778X/1] Funding Source: researchfish

向作者/读者索取更多资源

The ATP-binding cassette (ABC) transporters are primary transporters that couple the energy stored in adenosine triphosphate (ATP) to the movement of molecules across the membrane. ABC transporters can be divided into exporters and importers; importers mediate the uptake of essential nutrients into cells and are found predominantly in prokaryotes whereas exporters transport molecules out of cells or into organelles and are found in all organisms. ABC exporters have been linked with multi-drug resistance in both bacterial and eukaryotic cells. ABC transporters are powered by the hydrolysis of ATP and transport their substrate via the alternating access mechanism, whereby the protein alternates between a conformation in which the substrate-binding site is accessible from the outside of the membrane, outward-facing and one in which it is inward-facing. In this mini-review, the structures of different ABC transporter types in different conformations are presented within the context of the alternating access mechanism and how they have shaped our current understanding of the mechanism of ABC transporters.

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