2b10: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2b10.gif|left|200px]]<br /><applet load="2b10" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2b10, resolution 2.800&Aring;" />
-'''Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase'''<br />
-==Overview==
+==Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase==
-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 load='2b10' size='340' side='right'caption='[[2b10]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
-==About this Structure==
+==See Also==
-B10 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZNH and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B10 OCA].
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
-==Reference==
+__TOC__
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16227441 16227441]
+</StructureSection>
-[[Category: Cytochrome-c peroxidase]]
+[[Category: Large Structures]]
-[[Category: Protein complex]]
 [[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:30:38 2007''