Journal article
Structure and mechanism of ABC transporters.
- Locher KP Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland. locher@mol.biol.ethz.ch
- 2004-08-18
Published in:
- Current opinion in structural biology. - 2004
ATP-Binding Cassette Transporters
Escherichia coli Proteins
Hydrolysis
Models, Molecular
Periplasmic Binding Proteins
Protein Structure, Tertiary
Protein Transport
Structure-Activity Relationship
Vitamin B 12
English
ATP-binding cassette (ABC) transporters facilitate unidirectional translocation of chemically diverse substrates across cell or organelle membranes. The recently determined crystal structures of the vitamin B(12) importer BtuCD and its cognate binding protein BtuF have revealed critical architectural features that are probably shared by other ABC transporters. For example, the arrangement of the ABC domains and their interface with the membrane-spanning domains are probably conserved, whereas the number of transmembrane helices and their arrangement are not. Two distinct mechanistic schemes for how ABC engines couple ATP hydrolysis to substrate transport have been proposed recently and are being explored.
- Language
-
- English
- Open access status
- closed
- Identifiers
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- DOI 10.1016/j.sbi.2004.06.005
- PMID 15313236
- Persistent URL
- https://sonar.ch/global/documents/47162
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