5sw6 | pdb_00005sw6

Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6

spinqualitylabelsall models 5sw6, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5sw6 is a 2 chain structure with sequence from Burkholderia pseudomallei 1710b. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: HEM, MPD, NA, O, OXY, PO4 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. See Also Catalase 3D structures

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