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[[Image:2b10.gif|left|200px]]


{{Structure
==Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase==
|PDB= 2b10 |SIZE=350|CAPTION= <scene name='initialview01'>2b10</scene>, resolution 2.800&Aring;
<StructureSection load='2b10' size='340' side='right'caption='[[2b10]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
<table><tr><td colspan='2'>[[2b10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B10 FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE= CCP1, CCP, CPO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), CYC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b10 OCA], [https://pdbe.org/2b10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b10 RCSB], [https://www.ebi.ac.uk/pdbsum/2b10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b10 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b1/2b10_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b10 ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase'''
==See Also==
 
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
==Overview==
__TOC__
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.
</StructureSection>
 
[[Category: Large Structures]]
==About this Structure==
2B10 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B10 OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16227441 16227441]
[[Category: Cytochrome-c peroxidase]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Crane, B R.]]
[[Category: Crane BR]]
[[Category: Kang, S A.]]
[[Category: Kang SA]]
[[Category: HEM]]
[[Category: ZNH]]
[[Category: cytochrome]]
[[Category: electron transfer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:56:14 2008''

Latest revision as of 12:15, 14 February 2024

Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidaseCrystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase

Structural highlights

2b10 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2b10, resolution 2.80Å

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