1qgj

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Revision as of 22:33, 20 November 2007

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spinqualitylabelsall models 1qgj, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ARABIDOPSIS THALIANA PEROXIDASE N

Overview

The structure of the neutral peroxidase from Arabidopsis thaliana (ATP N), has been determined to a resolution of 1.9 A and a free R value of 20.5%., ATP N has the expected characteristic fold of the class III peroxidases, with a C(alpha) r.m.s.d. of 0.82 A when compared with horseradish, peroxidase C (HRP C). HRP C is 54% identical to ATP N in sequence. When, the structures of four class III plant peroxidases are superimposed, the, regions with structural differences are non-randomly distributed; all are, located in one half of the molecule. The architecture of the haem pocket, of ATP N is very similar to that of HRP C, in agreement with the low, small-molecule substrate specificity of all class III peroxidases. The, structure of ATP N suggests that the pH dependence of the substrate, turnover will differ from that of HRP C owing to differences in polarity, of the residues in the substrate-access channel. Since there are fewer, hydrogen bonds to haem C17 propionate O atoms in ATP N than in HRP C, it, is suggested that ATP N will lose haem more easily than HRP C. Unlike, almost all other class III plant peroxidases, ATP N has a free cysteine, residue at a similar position to the suggested secondary substrate-binding, site in lignin peroxidase.

About this Structure

1QGJ is a Single protein structure of sequence from Arabidopsis thaliana with CA, HEM and GSH as ligands. Full crystallographic information is available from OCA.

Reference

Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase., Mirza O, Henriksen A, Ostergaard L, Welinder KG, Gajhede M, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):372-5. PMID:10713531

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