This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 17: | Line 17: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[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
|
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
