2b0z: Difference between revisions

Revision as of 04:47, 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:2b0z.png

Template:STRUCTURE 2b0z

Crystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidaseCrystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidase

Template:ABSTRACT PUBMED 16227441

About this StructureAbout this Structure

2B0Z is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Effects of interface mutations on association modes and electron-transfer rates between proteins., Kang SA, Crane BR, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15465-70. Epub 2005 Oct 14. PMID:16227441

Page seeded by OCA on Mon Jul 28 04:47:38 2008

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OCA

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-'''Crystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidase'''
+===Crystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidase===
-==Overview==
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-Although bonding networks determine electron-transfer (ET) rates within proteins, the mechanism by which structure and dynamics influence ET across protein interfaces is not well understood. Measurements of photochemically induced ET and subsequent charge recombination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single crystals correlate reactivity with defined structures for different association modes of the redox partners. Structures and ET rates in crystals are consistent with tryptophan oxidation mediating charge recombination reactions. Conservative mutations at the interface can drastically affect how the proteins orient and dispose redox centers. Whereas some configurations are ET inactive, the wild-type complex exhibits the fastest recombination rate. Other association modes generate ET rates that do not correlate with predictions based on cofactor separations or simple bonding pathways. Inhibition of photoinduced ET at &lt;273 K indicates gating by small-amplitude dynamics, even within the crystal. Thus, different associations achieve states of similar reactivity, and within those states conformational fluctuations enable interprotein ET.
+The line below this paragraph, {{ABSTRACT_PUBMED_16227441}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16227441 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16227441}}
 ==About this Structure==
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 [[Category: Cytochrome]]
 [[Category: Electron transfer]]
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