1IPH

STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI

Summary for 1IPH

• Entry DOI: 10.2210/pdb1iph/pdb
• Descriptor: CATALASE HPII, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• Functional Keywords: hydrogen peroxide, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Probable): P21179
• Total number of polymer chains: 4
• Total formula weight: 339551.76

Authors

Bravo, J.,Loewen, P.C.,Fita, I. (deposition date: 1995-12-31, release date: 1997-09-04, Last modification date: 2023-09-27)

Primary citation

Bravo, J.,Verdaguer, N.,Tormo, J.,Betzel, C.,Switala, J.,Loewen, P.C.,Fita, I.
Crystal structure of catalase HPII from Escherichia coli.
Structure, 3:491-502, 1995

PubMed Abstract: Catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that are quite distinct from other catalases in physical structure and catalytic properties. HPII, studied in this work, is encoded by the katE gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic group per subunit of 753 residues.

PubMed: 7663946
DOI: 10.1016/S0969-2126(01)00182-4

Experimental method

X-RAY DIFFRACTION (2.8 Å)