1s6v: Difference between revisions

Revision as of 21:07, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s6v.png

Template:STRUCTURE 1s6v

Structure of a cytochrome c peroxidase-cytochrome c site specific cross-linkStructure of a cytochrome c peroxidase-cytochrome c site specific cross-link

Template:ABSTRACT PUBMED 15071191

About this StructureAbout this Structure

1S6V is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link., Guo M, Bhaskar B, Li H, Barrows TP, Poulos TL, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5940-5. Epub 2004 Apr 7. PMID:15071191

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c., Pelletier H, Kraut J, Science. 1992 Dec 11;258(5089):1748-55. PMID:1334573

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 {{STRUCTURE_1s6v|  PDB=1s6v  |  SCENE=  }}
-'''Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link'''
+===Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link===
-==Overview==
+<!--
-A specific covalently cross-linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c) has been made by engineering cysteines into CCP and cyt. c that form an intermolecular disulfide bond in high yield. The crystal structure of the cross-linked complex has been solved to 1.88-A resolution and closely resembles the structure of the noncovalent complex [Pellitier, H. &amp; Kraut, J. (1992) Science 258, 1748-1755]. The higher resolution of the covalent complex has enabled the location of ordered water molecules at the peroxidase-cytochrome c interface that serve to bridge between the two proteins by hydrogen bonding. As in the noncovalent complex, direct electrostatic interactions between protein groups appear not to be critical in complex formation. UV-visible spectroscopic and stopped-flow studies indicate that CCP in the covalent complex reacts normally with H(2)O(2) to give compound I. Stopped-flow kinetic studies also show that intramolecular electron transfer between the cross-linked ferrocytochrome c and the Trp-191 cation radical site in CCP compound I occurs fast and is nearly complete within the dead time ( approximately 2 ms) of the instrument. These results indicate that the structure of the covalent complex closely mimics the physiological electron transfer complex. In addition, single-turnover and steady-state experiments reveal that CCP compound I in the covalent complex oxidizes exogenously added ferrocytochrome c at a slow rate (t(1/2) approximately 2 min), indicating that CCP does not have a second independent site for physiologically relevant electron transfer.
+The line below this paragraph, {{ABSTRACT_PUBMED_15071191}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15071191}}
 ==About this Structure==
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 ==Reference==
 Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link., Guo M, Bhaskar B, Li H, Barrows TP, Poulos TL, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5940-5. Epub 2004 Apr 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15071191 15071191]
+Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c., Pelletier H, Kraut J, Science. 1992 Dec 11;258(5089):1748-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1334573 1334573]
 [[Category: Cytochrome-c peroxidase]]
 [[Category: Protein complex]]
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 [[Category: Heme enzyme]]
 [[Category: Oxidoreductase]]
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