1qgj
From Proteopedia
(New page: 200px<br /><applet load="1qgj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgj, resolution 1.90Å" /> '''ARABIDOPSIS THALIANA...) |
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| - | [[Image:1qgj.gif|left|200px]]<br /><applet load="1qgj" size=" | + | [[Image:1qgj.gif|left|200px]]<br /><applet load="1qgj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qgj, resolution 1.90Å" /> | caption="1qgj, resolution 1.90Å" /> | ||
'''ARABIDOPSIS THALIANA PEROXIDASE N'''<br /> | '''ARABIDOPSIS THALIANA PEROXIDASE N'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the neutral peroxidase from Arabidopsis thaliana (ATP N) | + | 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== | ==About this Structure== | ||
| - | 1QGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CA, HEM and GSH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mirza, O.]] | [[Category: Mirza, O.]] | ||
[[Category: Oestergaard, L.]] | [[Category: Oestergaard, L.]] | ||
| - | [[Category: Welinder, K | + | [[Category: Welinder, K G.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: GSH]] | [[Category: GSH]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:16 2008'' |
Revision as of 12:39, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 14:39:16 2008
Categories: Arabidopsis thaliana | Single protein | Gajhede, M. | Henriksen, A. | Mirza, O. | Oestergaard, L. | Welinder, K G. | CA | GSH | HEM | Oxidoreductase | Peroxidase
