2R6G

The Crystal Structure of the E. coli Maltose Transporter

Summary for 2R6G

• Entry DOI: 10.2210/pdb2r6g/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose/maltodextrin import ATP-binding protein malK, Maltose-binding periplasmic protein, Maltose transport system permease protein malF, ... (6 entities in total)
• Functional Keywords: abc transporter, catalytic intermediate, e. coli maltose transporter, mbp, maltodextrin binding protein, malk, atp binding cassette, atp-binding, hydrolase, inner membrane, membrane, nucleotide-binding, sugar transport, transmembrane, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 215776.04

Authors

Oldham, M.L.,Khare, D.,Quiocho, F.A.,Davidson, A.L.,Chen, J. (deposition date: 2007-09-05, release date: 2007-11-27, Last modification date: 2023-08-30)

Primary citation

Oldham, M.L.,Khare, D.,Quiocho, F.A.,Davidson, A.L.,Chen, J.
Crystal structure of a catalytic intermediate of the maltose transporter.
Nature, 450:515-521, 2007

PubMed 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.

PubMed: 18033289
DOI: 10.1038/nature06264

Experimental method

X-RAY DIFFRACTION (2.8 Å)