2r6g

The Crystal Structure of the E. coli Maltose Transporter

spinqualitylabelsall models 2r6g, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2r6g is a 5 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MAL Gene: malK (ECOLI), malE (ECOLI), malF (ECOLI), malG (ECOLI) Activity: Maltose-transporting ATPase, with EC number 3.6.3.19 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MALG_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [MALK_ECOUT] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system (By similarity). [MALF_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Maltose-binding protein

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