2b0z: Difference between revisions
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<StructureSection load='2b0z' size='340' side='right'caption='[[2b0z]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2b0z' size='340' side='right'caption='[[2b0z]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b0z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2b0z]] is a 2 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=2B0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B0Z FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=2b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0z OCA], [https://pdbe.org/2b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b0z RCSB], [https://www.ebi.ac.uk/pdbsum/2b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0z ProSAT]</span></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=2b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0z OCA], [https://pdbe.org/2b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b0z RCSB], [https://www.ebi.ac.uk/pdbsum/2b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Crane BR]] | ||
[[Category: | [[Category: Kang SA]] | ||
Revision as of 14:19, 22 May 2024
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
Structural highlights
FunctionCCPR_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. Publication Abstract from PubMedAlthough 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 <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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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