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2hv4

From Proteopedia

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{{Seed}}
 
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[[Image:2hv4.png|left|200px]]
 
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<!--
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==NMR solution structure refinement of yeast iso-1-ferrocytochrome c==
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The line below this paragraph, containing "STRUCTURE_2hv4", creates the "Structure Box" on the page.
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<StructureSection load='2hv4' size='340' side='right'caption='[[2hv4]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HV4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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-->
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ycc|1ycc]], [[1yfc|1yfc]]</div></td></tr>
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{{STRUCTURE_2hv4| PDB=2hv4 | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2hv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hv4 OCA], [https://pdbe.org/2hv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hv4 RCSB], [https://www.ebi.ac.uk/pdbsum/2hv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hv4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
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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/hv/2hv4_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=2hv4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein-protein interactions are driven by specific properties of the molecular surfaces. Cytochrome c, a small electron transfer protein, is involved in a number of biologically relevant interactions with macromolecular partners. Small molecules may interfere with such interactions by binding to the surface of cytochrome c. Here we investigated the possibility of weak intermolecular interactions between reduced cytochrome c and a library of 325 small molecules, using WaterLOGSY NMR spectroscopy. Specific binding was found for p-aminophenol. The solution structure of the p-aminophenol-cytochrome c adduct was determined using a combination of in silico tools and NMR-based restraints. The ligand interacts in a specific binding site on the protein surface through a combination of stacking and H-bond interactions. Small but meaningful rearrangements of the solvent-exposed side chains are observed upon ligand binding and contribute to the stabilization of the complex.
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===NMR solution structure refinement of yeast iso-1-ferrocytochrome c===
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Cytochrome c and organic molecules: solution structure of the p-aminophenol adduct.,Assfalg M, Bertini I, Del Conte R, Giachetti A, Turano P Biochemistry. 2007 May 29;46(21):6232-8. Epub 2007 May 9. PMID:17488096<ref>PMID:17488096</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2hv4" style="background-color:#fffaf0;"></div>
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<!--
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17488096}}, adds the Publication Abstract to the page
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17488096 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17488096}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Atcc 18824]]
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2HV4 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HV4 OCA].
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[[Category: Large Structures]]
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[[Category: Assfalg, M]]
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==Reference==
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[[Category: Bertini, I]]
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<ref group="xtra">PMID:17488096</ref><references group="xtra"/>
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[[Category: Conte, R Del]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Turano, P]]
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[[Category: Assfalg, M.]]
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[[Category: Bertini, I.]]
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[[Category: Conte, R Del.]]
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[[Category: Turano, P.]]
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[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Heme protein]]
[[Category: Heme protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:16:40 2009''
 

Current revision

NMR solution structure refinement of yeast iso-1-ferrocytochrome c

PDB ID 2hv4

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