2dri | pdb_00002dri

PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS

spinqualitylabelsall models 2dri, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2dri is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1dri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RIP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RBSB_ECOLI] Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis. 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 A number of mutations at Gly134 of the periplasmic ribose-binding protein of Escherichia coli were examined by a combined biochemical and structural approach. Different mutations gave rise to different patterns of effects on the chemotaxis and transport functions. The smallest residue (alanine) had the least effect on transport, whereas large hydrophobic residues had the smallest effect on chemotaxis. Comparison of the x-ray crystal structure of the G134R mutant protein (2.5-A resolution) to that of the wild type (1.6-A resolution) showed that the basic structure of the protein was unaltered. The loss of chemotaxis and transport functions in this and similar mutant proteins must therefore be caused by relatively simple surface effects, which include a change in local main chain conformation. The loss of chemotaxis and transport functions resulting from the introduction of an alanine residue at position 134 was suppressed by an additional isoleucine to threonine mutation at residue 132. An x-ray structure of the I132T/G134A double mutant protein (2.2-A resolution) showed that the changes in local structure were accompanied by a diffuse pattern of structural changes in the surrounding region, implying that the suppression derives from a combination of sources. Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis.,Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL J Biol Chem. 1994 Dec 2;269(48):30206-11. PMID:7982928 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribose-binding protein

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