2gbp | pdb_00002gbp

SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI GALACTOSE CHEMORECEPTOR PROTEIN

spinqualitylabelsall models 2gbp, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2gbp is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DGAL_ECOLI] This protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor. 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 D-galactose-binding (or chemoreceptor) protein of Escherichia coli serves as an initial component for both chemotaxis towards galactose and glucose and high-affinity active transport of the two sugars. Well-refined x-ray structures of the liganded forms of the wild-type and a mutant protein isolated from a strain defective in chemotaxis but fully competent in transport have provided a molecular view of the sugar-binding site and of a site for interacting with the Trg transmembrane signal transducer. The geometry of the sugar-binding site, located in the cleft between the two lobes of the bilobate protein, is novel in that it is designed for tight binding and sequestering of either the alpha or beta anomer of the D-stereoisomer of the 4-epimers galactose and glucose. Binding specificity and affinity are conferred primarily by polar planar side-chain residues that form intricate networks of cooperative and bidentate hydrogen bonds with the sugar substrates, and secondarily by aromatic residues that sandwich the pyranose ring. Each of the pairs of anomeric hydroxyls and epimeric hydroxyls is recognized by a distinct Asp residue. The site for interaction with the transducer is about 18 A from the sugar-binding site. Mutation of Gly74 to Asp at this site, concomitant with considerable changes in the local ordered water structures, contributes to the lack of productive interaction with the transmembrane signal transducer. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein.,Vyas NK, Vyas MN, Quiocho FA Science. 1988 Dec 2;242(4883):1290-5. PMID:3057628 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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