2cah

From Proteopedia

Revision as of 14:58, 30 October 2007

STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH

Overview

A catalase from a peroxide resistant mutant of Proteus mirabilis binds, NADPH tightly. Interestingly, this enzyme can be stripped of NADPH without, loss of the catalatic activity. It is the only known non-mammalian, catalase able to bind NADPH. The structure without cofactor was solved by, molecular replacement using the structure of beef liver catalase as a, model. The structure was refined to an R-factor of 19.3% in the range 8 to, 2.2 A resolution. According to the sequence, a methionine sulphone was, positioned in the haem active site. This oxidized form of methionine is, particular to Proteus mirabilis catalase and likely to produce some steric, hindrance in the active site. Two important water molecules are positioned, in the haem distal site. These two water molecules are not ... [(full description)]

About this Structure

2CAH is a [Single protein] structure of sequence from [Proteus mirabilis] with HEM and NDP as [ligands]. This structure superseeds the now removed PDB entry 1CAF. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Sites: 337 and 54. Full crystallographic information is available from [OCA].

Reference

Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH., Gouet P, Jouve HM, Dideberg O, J Mol Biol. 1995 Jun 23;249(5):933-54. PMID:7791219

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