1qgj

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[[Image:1qgj.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1qgj", creates the "Structure Box" on the page.
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgj OCA], [http://www.ebi.ac.uk/pdbsum/1qgj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgj RCSB]</span>
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'''ARABIDOPSIS THALIANA PEROXIDASE N'''
'''ARABIDOPSIS THALIANA PEROXIDASE N'''
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[[Category: Oestergaard, L.]]
[[Category: Oestergaard, L.]]
[[Category: Welinder, K G.]]
[[Category: Welinder, K G.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: peroxidase]]
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[[Category: Peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:14:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:13 2008''
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Revision as of 03:14, 3 May 2008

Image:1qgj.gif

Template:STRUCTURE 1qgj

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. 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 Page seeded by OCA on Sat May 3 06:14:29 2008

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