Mechanistic diversity in ATP-binding cassette (ABC) transporters.
- Locher KP Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, Zurich, Switzerland.
- 2016-06-09
Published in:
- Nature structural & molecular biology. - 2016
ATP-Binding Cassette Transporters
Adenosine Triphosphate
Animals
Bacteria
Biological Transport
Catalytic Domain
Gene Expression
Humans
Hydrolysis
Models, Molecular
Protein Binding
Protein Domains
Protein Folding
Protein Structure, Secondary
English
ABC transporters catalyze transport reactions, such as the high-affinity uptake of micronutrients into bacteria and the export of cytotoxic compounds from mammalian cells. Crystal structures of ABC domains and full transporters have provided a framework for formulating reaction mechanisms of ATP-driven substrate transport, but recent studies have suggested remarkable mechanistic diversity within this protein family. This review evaluates the differing mechanistic proposals and outlines future directions for the exploration of ABC-transporter-catalyzed reactions.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1038/nsmb.3216
- PMID 27273632
- Persistent URL
- https://sonar.ch/global/documents/277238
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