2r6g
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. 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 Page seeded by OCA on Sun May 4 16:19:32 2008
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- Escherichia coli
- Maltose-transporting ATPase
- Protein complex
- Chen, J.
- Davidson, A L.
- Khare, D.
- Oldham, M L
- Quiocho, F A.
- Abc transporter
- Atp binding cassette
- Atp-binding
- Catalytic intermediate
- E. coli maltose transporter
- Hydrolase
- Hydrolase/transport protein complex
- Inner membrane
- Malk
- Maltodextrin binding protein
- Mbp
- Membrane
- Nucleotide-binding
- Periplasm
- Sugar transport
- Transmembrane