1h7k

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spinqualitylabelsall models 1h7k, resolution 2.4Å 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

Proteus mirabilis catalase (PMC) belongs to the family of NADPH binding, catalases. The function of NADPH in these enzymes is still a matter of, debate. This study presents the effects of two independent phenylalanine, mutations (F194 and F215), located between NADPH and heme in the PMC, structure. The phenylalanines were replaced with tyrosines which we, predicted could carry radicals in a NADPH-heme electron transfer. The, X-ray crystal structures of the two mutants indicated that neither the, binding site of NADPH nor the immediate environment of the residues was, affected by the mutations. Measurements using H2O2 as a substrate, confirmed that the variants were as active as the native enzyme. With, equivalent amounts of peroxoacetic acid, wild-type PMC, F215Y PMC, and, beef liver ... [(full description)]

About this Structure

1H7K is a [Single protein] structure of sequence from [Proteus mirabilis] with ACT, SO4 and HEM as [ligands]. Active as [[1]], with EC number [1.11.1.6]. Full crystallographic information is available from [OCA].

Reference

Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity., Andreoletti P, Gambarelli S, Sainz G, Stojanoff V, White C, Desfonds G, Gagnon J, Gaillard J, Jouve HM, Biochemistry. 2001 Nov 13;40(45):13734-43. PMID:11695923

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