1dcc
From Proteopedia
(New page: 200px<br /><applet load="1dcc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcc, resolution 2.2Å" /> '''2.2 ANGSTROM STRUCTUR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dcc.gif|left|200px]]<br /><applet load="1dcc" size=" | + | [[Image:1dcc.gif|left|200px]]<br /><applet load="1dcc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dcc, resolution 2.2Å" /> | caption="1dcc, resolution 2.2Å" /> | ||
'''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''<br /> | '''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Fe+3-OOH complex of peroxidases has a very short half life, and its | + | The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion. |
==About this Structure== | ==About this Structure== | ||
| - | 1DCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with OXY and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http:// | + | 1DCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCC OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kraut, J.]] | [[Category: Kraut, J.]] | ||
| - | [[Category: Miller, M | + | [[Category: Miller, M A.]] |
[[Category: Shaw, A.]] | [[Category: Shaw, A.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| Line 21: | Line 21: | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:10 2008'' |
Revision as of 10:15, 21 February 2008
|
2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX
Overview
The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion.
About this Structure
1DCC is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
Reference
2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex., Miller MA, Shaw A, Kraut J, Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080
Page seeded by OCA on Thu Feb 21 12:15:10 2008
