1dcc

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[[Image:1dcc.gif|left|200px]]
[[Image:1dcc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dcc |SIZE=350|CAPTION= <scene name='initialview01'>1dcc</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1dcc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1dcc| PDB=1dcc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcc OCA], [http://www.ebi.ac.uk/pdbsum/1dcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dcc RCSB]</span>
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}}
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'''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''
'''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''
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[[Category: Miller, M A.]]
[[Category: Miller, M A.]]
[[Category: Shaw, A.]]
[[Category: Shaw, A.]]
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[[Category: oxidoreductase(h2o2(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:41:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:49 2008''
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Revision as of 10:41, 2 May 2008

Template:STRUCTURE 1dcc

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. 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 Fri May 2 13:41:11 2008

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