1iph
STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI
|
OverviewOverview
BACKGROUND: 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. RESULTS: The, crystal structure of catalase HPII from E. coli has been determined to 2.8, A resolution. The asymmetric unit of the crystal contains a whole, molecule, which is a tetramer with accurate 222 point group symmetry. In, the model ... [(full description)]
About this StructureAbout this Structure
1IPH is a [Single protein] structure of sequence from [Escherichia coli] with HEM as [ligand]. The following page contains interesting information on the relation of 1IPH with [Catalase]. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Sites: CAA, CAB, CAC and CAD. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of catalase HPII from Escherichia coli., Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I, Structure. 1995 May 15;3(5):491-502. PMID:7663946
Page seeded by OCA on Tue Oct 30 13:47:49 2007