1u74: Difference between revisions

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[[Image:1u74.jpg|left|200px]]
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{{STRUCTURE_1u74|  PDB=1u74  |  SCENE=  }}
'''Electron Transfer Complex between cytochrome C and cytochrome C peroxidase'''


==Electron Transfer Complex between cytochrome C and cytochrome C peroxidase==
<StructureSection load='1u74' size='340' side='right'caption='[[1u74]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1u74]] 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=1U74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U74 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]] 2.4&#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=PO4:PHOSPHATE+ION'>PO4</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=1u74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u74 OCA], [https://pdbe.org/1u74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u74 RCSB], [https://www.ebi.ac.uk/pdbsum/1u74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u74 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/u7/1u74_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1u74 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form an important redox pair for understanding interprotein electron transfer (ET). Measurements of ET rates from photoexcited CcP substituted with Zn porphyrin to either yeast Fe(III)Cc or horse Fe(III)Cc in crystals reveal that the molecular associations found in the respective crystal structures determine solution reactivity. Similar forward rates for yeast isozyme-1 Cc (yCc) and yCc homologue horse Cc (hCc), despite different orientations relative to CcP, suggest small-amplitude conformational gating of ET even in the crystalline state; faster back ET in the yCc compared to the hCc complex agrees with the relative coupling between redox sites predicted by the structures.


==Overview==
Electron transfer between cytochrome c and cytochome c peroxidase in single crystals.,Kang SA, Marjavaara PJ, Crane BR J Am Chem Soc. 2004 Sep 8;126(35):10836-7. PMID:15339156<ref>PMID:15339156</ref>
Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form an important redox pair for understanding interprotein electron transfer (ET). Measurements of ET rates from photoexcited CcP substituted with Zn porphyrin to either yeast Fe(III)Cc or horse Fe(III)Cc in crystals reveal that the molecular associations found in the respective crystal structures determine solution reactivity. Similar forward rates for yeast isozyme-1 Cc (yCc) and yCc homologue horse Cc (hCc), despite different orientations relative to CcP, suggest small-amplitude conformational gating of ET even in the crystalline state; faster back ET in the yCc compared to the hCc complex agrees with the relative coupling between redox sites predicted by the structures.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1U74 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=1U74 OCA].
</div>
<div class="pdbe-citations 1u74" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Electron transfer between cytochrome c and cytochome c peroxidase in single crystals., Kang SA, Marjavaara PJ, Crane BR, J Am Chem Soc. 2004 Sep 8;126(35):10836-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15339156 15339156]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
[[Category: Protein complex]]
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Crane, B R.]]
[[Category: Crane BR]]
[[Category: Kang, S A.]]
[[Category: Kang SA]]
[[Category: Heme]]
[[Category: Protein-protein complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:50:18 2008''

Latest revision as of 07:16, 13 August 2026

Electron Transfer Complex between cytochrome C and cytochrome C peroxidase

1u74, resolution 2.40Å

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