1oaf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1oaf.gif|left|200px]] | [[Image:1oaf.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1oaf", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1oaf| PDB=1oaf | SCENE= }} | ||
}} | |||
'''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | ||
| Line 29: | Line 26: | ||
[[Category: Raven, E L.]] | [[Category: Raven, E L.]] | ||
[[Category: Sharp, K H.]] | [[Category: Sharp, K H.]] | ||
[[Category: | [[Category: Ascorbate peroxidase]] | ||
[[Category: | [[Category: Heme peroxidase]] | ||
[[Category: | [[Category: Peroxide scavenge]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:41 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 00:35, 3 May 2008
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 Page seeded by OCA on Sat May 3 03:35:41 2008