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- Title
Crystal structure of a catalytic intermediate of the maltose transporter.
- Authors
Oldham, Michael L; Khare, Dheeraj; Quiocho, Florante A; Davidson, Amy L; Chen, Jue
- Abstract
The maltose uptake system of Escherichia coli is a well-characterized member of the ATP-binding cassette transporter superfamily. Here we present the 2.8-A crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP. This structure, stabilized by a mutation that prevents ATP hydrolysis, captures the ATP-binding cassette dimer in a closed, ATP-bound conformation. Maltose is occluded within a solvent-filled cavity at the interface of the two transmembrane subunits, about halfway into the lipid bilayer. The binding protein docks onto the entrance of the cavity in an open conformation and serves as a cap to ensure unidirectional translocation of the sugar molecule. These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP.
- Publication
Nature, 2007, Vol 450, Issue 7169, p515
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature06264