1kok
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HIF:FE(III)-(4-MESOPORPHYRINONE)'>HIF</scene> | |LIGAND= <scene name='pdbligand=HIF:FE(III)-(4-MESOPORPHYRINONE)'>HIF</scene> | ||
| - | |ACTIVITY= [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] | + | |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> |
|GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2cyp|2CYP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kok OCA], [http://www.ebi.ac.uk/pdbsum/1kok PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kok RCSB]</span> | ||
}} | }} | ||
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[[Category: Immoos, C E.]] | [[Category: Immoos, C E.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
| - | [[Category: HIF]] | ||
[[Category: bifunctional catalyst]] | [[Category: bifunctional catalyst]] | ||
[[Category: cytochrome c peroxidase]] | [[Category: cytochrome c peroxidase]] | ||
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[[Category: trp191 cationic radical]] | [[Category: trp191 cationic radical]] | ||
| - | ''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 21:51:25 2008'' |
Revision as of 18:51, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | OPBYC (Saccharomyces cerevisiae) | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Related: | 2CYP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)
Overview
The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.
About this Structure
1KOK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases., Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL, J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:12237229
Page seeded by OCA on Sun Mar 30 21:51:25 2008
Categories: Cytochrome-c peroxidase | Saccharomyces cerevisiae | Single protein | Barrows, T P. | Bhaskar, B. | Cohen, M S. | Farmer, P J. | Immoos, C E. | Poulos, T L. | Bifunctional catalyst | Cytochrome c peroxidase | Cytochrome oxidase | Mesoporphyrin | Nitrite reducatse | Proximal loop | Trp191 cationic radical
