5sx3

Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5

spinqualitylabelsall models 5sx3, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5sx3 is a 2 chain structure. This structure supersedes the now removed PDB entry 2fxg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, HEM, MPD, NA, OXY Related: 5l02, 5l05, 5sw4, 5sw5, 5sw6, 5sx0, 5sx1, 5sx2, 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 Crystals of Burkholderia pseudomallei KatG retain their ability to diffract X-rays at high resolution after adjustment of the pH from 5.6 to 4.5, 6.5, 7.5, and 8.5, providing a unique view of the effect of pH on protein structure. One significant pH-sensitive change lies in the appearance of a perhydroxy group attached to the indole nitrogen of the active site Trp111 above pH 7, similar to a modification originally observed in the Ser324Thr variant of the enzyme at pH 5.6. The modification forms rapidly from molecular oxygen in the buffer with 100% occupancy after one minute of soaking of the crystal at room temperature and pH 8.5. The low temperature (4 K) ferric EPR spectra of the resting enzyme, being very sensitive to changes in the heme iron microenvironment, confirm the presence of the modification above pH 7 in native enzyme and variants lacking Arg426 or Met264 and its absence in variants lacking Trp111 or Tyr238. The indole-perhydroxy group is very likely the reactive intermediate of molecular oxygen in the NADH oxidase reaction, and Arg426 is required for its reduction. The second significant pH-sensitive change involves the buried side chain of Arg426 that changes from one predominant conformation at low pH to a second at high pH. The pH profiles of the peroxidase, catalase, and NADH oxidase reactions can be correlated with the distribution of Arg426 conformations. Other pH-induced structural changes include a number of surface-situated side chains, but there is only one change involving a displacement of main chain atoms triggered by the protonation of His53 in a deep pocket in the vicinity of the molecular 2-fold axis. Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.,Carpena X, Wiseman B, Deemagarn T, Herguedas B, Ivancich A, Singh R, Loewen PC, Fita I Biochemistry. 2006 Apr 25;45(16):5171-9. PMID:16618106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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