5jvo | pdb_00005jvo

Crystal structure of the Arginine Repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis

spinqualitylabelsall models 5jvo, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jvo is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, TYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A0E3UAP8_CORPS] Regulates arginine biosynthesis genes.[HAMAP-Rule:MF_00173] Publication Abstract from PubMed The arginine repressor (ArgR) regulates arginine biosynthesis in a number of microorganisms and consists of two domains interlinked by a short peptide; the N-terminal domain is involved in DNA binding and the C-terminal domain binds arginine and forms a hexamer made-up of a dimer of trimers. The crystal structure of the C-terminal domain of ArgR from the pathogenic Corynebacterium pseudotuberculosis determined at 1.9 A resolution contains a tightly bound tyrosine at the arginine-binding site indicating hitherto unobserved promiscuity. Structural analysis of the binding pocket displays clear molecular adaptations to accommodate tyrosine binding suggesting the possible existence of an alternative regulatory process in this pathogenic bacterium. Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis.,Mariutti RB, Ullah A, Araujo GC, Murakami MT, Arni RK Biochem Biophys Res Commun. 2016 Jul 8;475(4):350-5. doi:, 10.1016/j.bbrc.2016.05.091. Epub 2016 May 24. PMID:27233609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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