1cck
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1CCK 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 HEM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1CCK 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 HEM as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CCK OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7703247 7703247] | Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7703247 7703247] | ||
| + | [[Category: Cytochrome-c peroxidase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:50:02 2007'' |
Revision as of 08:45, 30 October 2007
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ALTERING SUBSTRATE SPECIFICITY OF CYTOCHROME C PEROXIDASE TOWARDS A SMALL MOLECULAR SUBSTRATE PEROXIDASE BY SUBSTITUTING TYROSINE FOR PHE 202
Overview
The crystal structure of recombinant pea cytosolic ascorbate peroxidase, has been refined to an R = 0.19 for data between 8.0 and 2.2 A resolution, and magnitude of F > or = 2 sigma(magnitude of F). The refined model, consists of four ascorbate peroxidase monomers consisting of 249 residues, per monomer assembled into two homodimers, with one heme group per, monomer. The ascorbate peroxidase model confirms that the pea cytosolic, enzyme is a noncovalent homodimer held together by a series of ionic, interactions arranged around the 2-fold noncrystallographic dimer axis. As, expected from the high level of sequence identity (33%), the overall fold, of the ascorbate peroxidase monomer closely resembles that of cytochrome c, peroxidase. The average root mean square differences for 137 ... [(full description)]
About this Structure
1CCK is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM as [ligand]. Active as [Cytochrome-c peroxidase], with EC number [1.11.1.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
Reference
Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:7703247
Page seeded by OCA on Tue Oct 30 10:50:02 2007
