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TitleRoles 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.
Journal, issue, pagesBiochemistry, Vol. 45, Page 5171-5179, Year 2006
Publish dateAug 9, 2016 (structure data deposition date)
AuthorsCarpena, X. / Wiseman, B. / Deemagarn, T. / Herguedas, B. / Ivancich, A. / Singh, R. / Loewen, P.C. / Fita, I.
External linksPubMed:16618106
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-5sx3:
Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5sx6:
Crystal structure of the catalase-peroxidase KatG of B. pseudomallei at pH 6.5
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5sx7:
Crystal structure of catalase-peroxidase KatG of B. pseudomallei at pH 8.5
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • burkholderia pseudomallei (strain 1710b) (bacteria)
KeywordsOXIDOREDUCTASE / catalase-peroxidase / KatG / pH changes / KatG oxidoreductase

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