1oaf
From Proteopedia
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| - | [[Image:1oaf.gif|left|200px]] | + | [[Image:1oaf.gif|left|200px]] |
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| - | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | + | {{Structure |
| + | |PDB= 1oaf |SIZE=350|CAPTION= <scene name='initialview01'>1oaf</scene>, resolution 1.4Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Asc+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=ASC:ASCORBIC ACID'>ASC</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OAF is a [ | + | 1OAF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAF OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:[http:// | + | Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12640445 12640445] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: L-ascorbate peroxidase]] | [[Category: L-ascorbate peroxidase]] | ||
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[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:04 2008'' |
Revision as of 11:08, 20 March 2008
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| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | L-ascorbate peroxidase, with EC number 1.11.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE
Overview
Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse--most peroxidases oxidize small organic substrates, but there are prominent exceptions--and there is a notable absence of structural information for a representative peroxidase-substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase-ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
About this Structure
1OAF is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:12640445
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