Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli

Acta Crystallographica. Section D, Biological Crystallography
Xavier CarpenaIgnacio Fita

Abstract

Catalase-peroxidases or KatGs, the apparent in vivo activators of the anti-tubercular pro-drug isoniazid, are active as homodimers, each subunit having two distinct but sequence- and structure-related domains. The N-terminal domain contains the haem group and is catalytically active, while the C-terminal domain lacks the cofactor. The C-terminal domain of KatG from Escherichia coli is expressed as a soluble protein which has been crystallized in triclinic, orthorhombic and tetragonal crystal forms. Packing in the orthorhombic crystals, with eight molecules in the asymmetric unit, follows the pattern of commensurate modulated structures, which explains the diversity of pseudo-origin peaks observed in the native Patterson map. The different crystal forms arise from variations in the length and sequence of the N-terminal extensions in the different constructs. Despite the variability in the N-terminal region, the overall domain conformations beginning with Pro437 are very similar both to each other and to the C-terminal domains within the native structures of the KatGs from Haloarcula marismortui and Burkholderia pseudomallei. Some structural reorganization in the C-terminal domain relative to the N-terminal domain has evolved to ...Continue Reading

Citations

May 24, 2008·Antioxidants & Redox Signaling·Marcel ZamockyChristian Obinger
Jul 27, 2010·Biochimica Et Biophysica Acta·Srijib BanerjeeChristian Obinger
Mar 13, 2015·Applied Microbiology and Biotechnology·Nikola Lončar, Marco W Fraaije
May 23, 2012·Archives of Biochemistry and Biophysics·Surabhi Mishra, James Imlay
Jan 3, 2012·Archives of Biochemistry and Biophysics·Adelaida DíazXavi Carpena
May 9, 2013·Applied Microbiology and Biotechnology·Patrizia Di GennaroGuido Sello

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