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| | {{STRUCTURE_1zzh| PDB=1zzh | SCENE= }} | | {{STRUCTURE_1zzh| PDB=1zzh | SCENE= }} |
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| - | '''Structure of the fully oxidized di-heme cytochrome c peroxidase from R. capsulatus'''
| + | ===Structure of the fully oxidized di-heme cytochrome c peroxidase from R. capsulatus=== |
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| - | ==Overview==
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| - | Cytochrome c peroxidases (CCP) play a key role in cellular detoxification by catalyzing the reduction of hydrogen peroxide to water. The di-heme CCP from Rhodobacter capsulatus is the fastest enzyme (1060 s(-1)), when tested with its physiological cytochrome c substrate, among all di-heme CCPs characterized to date and has, therefore, been an attractive target to investigate structure-function relationships for this family of enzymes. Here, we combine for the first time structural studies with site-directed mutagenesis and spectroscopic studies of the mutant enzymes to investigate the roles of amino acid residues that have previously been suggested to be important for activity. The crystal structure of R. capsulatus at 2.7 Angstroms in the fully oxidized state confirms the overall molecular scaffold seen in other di-heme CCPs but further reveals that a segment of about 10 amino acids near the peroxide binding site is disordered in all four molecules in the asymmetric unit of the crystal. Structural and sequence comparisons with other structurally characterized CCPs suggest that flexibility in this part of the molecular scaffold is an inherent molecular property of the R. capsulatus CCP and of CCPs in general and that it correlates with the levels of activity seen in CCPs characterized, thus, far. Mutagenesis studies support the spin switch model and the roles that Met-118, Glu-117, and Trp-97 play in this model. Our results help to clarify a number of aspects of the debate on structure-function relationships in this family of bacterial CCPs and set the stage for future studies.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16314410}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16314410 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16314410}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cytochrome c peroxidase]] | | [[Category: Cytochrome c peroxidase]] |
| | [[Category: Heme group]] | | [[Category: Heme group]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:16:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:39:06 2008'' |
Revision as of 10:39, 29 July 2008
Template:STRUCTURE 1zzh
Structure of the fully oxidized di-heme cytochrome c peroxidase from R. capsulatus
Template:ABSTRACT PUBMED 16314410
About this Structure
Full crystallographic information is available from OCA.
Reference
Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases., De Smet L, Savvides SN, Van Horen E, Pettigrew G, Van Beeumen JJ, J Biol Chem. 2006 Feb 17;281(7):4371-9. Epub 2005 Nov 28. PMID:16314410
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