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1s6v

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(New page: 200px<br /><applet load="1s6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6v, resolution 1.88&Aring;" /> '''Structure of a cytoc...)
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[[Image:1s6v.jpg|left|200px]]<br /><applet load="1s6v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s6v, resolution 1.88&Aring;" />
 
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'''Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link'''<br />
 
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==Overview==
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==Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link==
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A specific covalently cross-linked complex between redox partners yeast, cytochrome c peroxidase (CCP) and cytochrome c (cyt. c) has been made by, engineering cysteines into CCP and cyt. c that form an intermolecular, disulfide bond in high yield. The crystal structure of the cross-linked, complex has been solved to 1.88-A resolution and closely resembles the, structure of the noncovalent complex [Pellitier, H. &amp; Kraut, J. (1992), Science 258, 1748-1755]. The higher resolution of the covalent complex has, enabled the location of ordered water molecules at the, peroxidase-cytochrome c interface that serve to bridge between the two, proteins by hydrogen bonding. As in the noncovalent complex, direct, electrostatic interactions between protein groups appear not to be, critical in complex formation. UV-visible spectroscopic and stopped-flow, studies indicate that CCP in the covalent complex reacts normally with, H(2)O(2) to give compound I. Stopped-flow kinetic studies also show that, intramolecular electron transfer between the cross-linked ferrocytochrome, c and the Trp-191 cation radical site in CCP compound I occurs fast and is, nearly complete within the dead time ( approximately 2 ms) of the, instrument. These results indicate that the structure of the covalent, complex closely mimics the physiological electron transfer complex. In, addition, single-turnover and steady-state experiments reveal that CCP, compound I in the covalent complex oxidizes exogenously added, ferrocytochrome c at a slow rate (t(1/2) approximately 2 min), indicating, that CCP does not have a second independent site for physiologically, relevant electron transfer.
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<StructureSection load='1s6v' size='340' side='right'caption='[[1s6v]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s6v]] 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=1S6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
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<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=IOD:IODIDE+ION'>IOD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6v OCA], [https://pdbe.org/1s6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6v RCSB], [https://www.ebi.ac.uk/pdbsum/1s6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s6/1s6v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1s6v ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1S6V 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 IOD 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=1S6V OCA].
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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==Reference==
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__TOC__
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Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link., Guo M, Bhaskar B, Li H, Barrows TP, Poulos TL, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5940-5. Epub 2004 Apr 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15071191 15071191]
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</StructureSection>
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[[Category: Cytochrome-c peroxidase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Barrows, T.P.]]
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[[Category: Barrows TP]]
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[[Category: Bhaskar, B.]]
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[[Category: Bhaskar B]]
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[[Category: Guo, M.]]
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[[Category: Guo M]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos TL]]
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[[Category: HEM]]
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[[Category: IOD]]
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[[Category: electron transfer]]
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[[Category: heme enzyme]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:09:28 2007''
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Current revision

Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link

PDB ID 1s6v

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