2r6g

File:2r6g.jpg

spinqualitylabelsall models 2r6g, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The Crystal Structure of the E. coli Maltose Transporter

OverviewOverview

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.

About this StructureAbout this Structure

2R6G is a Protein complex structure of sequences from Escherichia coli with and as ligands. Active as Maltose-transporting ATPase, with EC number 3.6.3.19 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a catalytic intermediate of the maltose transporter., Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J, Nature. 2007 Nov 22;450(7169):515-21. PMID:18033289

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