1oaf
From Proteopedia
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|PDB= 1oaf |SIZE=350|CAPTION= <scene name='initialview01'>1oaf</scene>, resolution 1.4Å | |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> | |SITE= <scene name='pdbsite=AC1:Asc+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaf OCA], [http://www.ebi.ac.uk/pdbsum/1oaf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oaf RCSB]</span> | ||
}} | }} | ||
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[[Category: Raven, E L.]] | [[Category: Raven, E L.]] | ||
[[Category: Sharp, K H.]] | [[Category: Sharp, K H.]] | ||
| - | [[Category: ASC]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: NA]] | ||
[[Category: ascorbate peroxidase]] | [[Category: ascorbate peroxidase]] | ||
[[Category: heme peroxidase]] | [[Category: heme peroxidase]] | ||
[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:17 2008'' |
Revision as of 19:42, 30 March 2008
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| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | L-ascorbate peroxidase, with EC number 1.11.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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