PMID:21566157
| Citation |
Oldham, ML and Chen, J (2011) Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science 332:1202-5 |
|---|---|
| Abstract |
Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert chemical energy from ATP hydrolysis to mechanical work for substrate translocation. They function by alternating between two states, exposing the substrate-binding site to either side of the membrane. A key question that remains to be addressed is how substrates initiate the transport cycle. Using x-ray crystallography, we have captured the maltose transporter in an intermediate step between the inward- and outward-facing states. We show that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state. These results, interpreted in light of biochemical and functional studies, provide a structural basis to understand allosteric communication in ABC transporters. |
| Links |
PubMed Online version:10.1126/science.1200767 |
| Keywords |
ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs; Binding Sites; Biological Transport, Active; Catalytic Domain; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrogen Bonding; Maltose/metabolism; Maltose-Binding Proteins/chemistry; Maltose-Binding Proteins/metabolism; Models, Biological; Models, Molecular; Monosaccharide Transport Proteins/chemistry; Monosaccharide Transport Proteins/metabolism; Periplasm/metabolism; Protein Conformation; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary |
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