1oib | pdb_00001oib

PHOSPHATE-BINDING PROTEIN MUTANT T141D

spinqualitylabelsall models 1oib, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oib is a 2 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. Gene: PHOS ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import. 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 Electrostatic interactions are among the key forces determining the structure and function of proteins. These are exemplified in the liganded form of the receptor, a phosphate binding protein from Escherichia coli. The phosphate, completely dehydrated and buried in the receptor, is bound by 12 hydrogen bonds as well as a salt link with Arg 135. We have modulated the ionic attraction while preserving the hydrogen bonds by mutating Asp 137, also salt linked to Arg 135, to Asn, Gly or Thr. High-resolution crystallographic analysis revealed that Gly and Thr (but not Asn) mutant proteins have incorporated a more electronegative Cl- in place of the Asp carboxylate. That no dramatic effect on phosphate affinity was produced by these ionic perturbations indicates a major role for hydrogen bonds and other local dipoles in the binding and charge stabilization of ionic ligands. Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.,Yao N, Ledvina PS, Choudhary A, Quiocho FA Biochemistry. 1996 Feb 20;35(7):2079-85. PMID:8652549 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphate-binding protein

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