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spinqualitylabelsall models 1h6n, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

FORMATION OF A TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE BY DIRECTED MUTAGENESIS AND CONSEQUENCES FOR NUCLEOTIDE REACTIVITY

Overview

Heme catalases are homotetrameric enzymes with a highly conserved complex, quaternary structure, and their functional role is still not well, understood. Proteus mirabilis catalase (PMC), a heme enzyme belonging to, the family of NADPH-binding catalases, was efficiently overexpressed in E., coli. The recombinant catalase (rec PMC) was deficient in heme with, one-third heme and two-thirds protoporphyrin IX as determined by mass, spectrometry and chemical methods. This ratio was influenced by the, expression conditions, but the enzyme-specific activity calculated, relative to the heme content remained unchanged. The crystal structure of, rec PMC was solved to a resolution of 2.0 A, the highest resolution, obtained to date with PMC. The overall structure was quite similar to that, of ... [(full description)]

About this Structure

1H6N is a [Single protein] structure of sequence from [Proteus mirabilis] with ACT, SO4 and HEM as [ligands]. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Site: HEM. Full crystallographic information is available from [OCA].

Reference

High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron., Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM, Proteins. 2003 Feb 1;50(2):261-71. PMID:12486720

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