5sx0 | pdb_00005sx0

Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5

spinqualitylabelsall models 5sx0, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5sx0 is a 2 chain structure. This structure supersedes the now removed PDB entry 2b2s. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, MPD, NA, O, OXY, TRS NonStd Res: MHO Related: 5l02, 5l05, 5sw4, 5sw5, 5sw6, 5sx1, 5sx2, 5sx3, 5sx6, 5sx7, 5sxq, 5sxr, 5sxs, 5sxt, 5sxx, 5syh, 5syi, 5syj, 5syk, 5syl, 5syu, 5syv, 5syw, 5syx, 5syy Activity: Catalase peroxidase, with EC number 1.11.1.21 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KATG_BURP1] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Publication Abstract from PubMed The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp. A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.,Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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