5syk

Crystal structure of B. pseudomallei KatG treated with hydrogen peroxide

spinqualitylabelsall models 5syk, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5syk 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 1.8Å Ligands: CL, HEM, MPD, MRD, NA, OXY, TOX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KATG_BURPS Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity. Publication Abstract from PubMed Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatG's involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp. An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.,Loewen PC, Carpena X, Vidossich P, Fita I, Rovira C J Am Chem Soc. 2014 May 21;136(20):7249-52. doi: 10.1021/ja502794e. Epub 2014 May, 7. PMID:24785434 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catalase 3D structures

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