3cus

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{{Seed}}
 
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[[Image:3cus.png|left|200px]]
 
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==Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution==
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The line below this paragraph, containing "STRUCTURE_3cus", creates the "Structure Box" on the page.
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<StructureSection load='3cus' size='340' side='right'caption='[[3cus]], [[Resolution|resolution]] 2.20&Aring;' 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'>[[3cus]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Solidesulfovibrio_fructosivorans Solidesulfovibrio fructosivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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{{STRUCTURE_3cus| PDB=3cus | SCENE= }}
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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=3cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cus OCA], [https://pdbe.org/3cus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cus RCSB], [https://www.ebi.ac.uk/pdbsum/3cus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cus ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHNS_SOLFR PHNS_SOLFR] Involved in hydrogen uptake for the anaerobic reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is the physiological electron acceptor.
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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/cu/3cus_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3cus 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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Hydrogenases, which catalyze H(2) to H(+) conversion as part of the bioenergetic metabolism of many microorganisms, are among the metalloenzymes for which a gas-substrate tunnel has been described by using crystallography and molecular dynamics. However, the correlation between protein structure and gas-diffusion kinetics is unexplored. Here, we introduce two quantitative methods for probing the rates of diffusion within hydrogenases. One uses protein film voltammetry to resolve the kinetics of binding and release of the competitive inhibitor CO; the other is based on interpreting the yield in the isotope exchange assay. We study structurally characterized mutants of a NiFe hydrogenase, and we show that two mutations, which significantly narrow the tunnel near the entrance of the catalytic center, decrease the rates of diffusion of CO and H(2) toward and from the active site by up to 2 orders of magnitude. This proves the existence of a functional channel, which matches the hydrophobic cavity found in the crystal. However, the changes in diffusion rates do not fully correlate with the obstruction induced by the mutation and deduced from the x-ray structures. Our results demonstrate the necessity of measuring diffusion rates and emphasize the role of side-chain dynamics in determining these.
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===Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution===
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Experimental approaches to kinetics of gas diffusion in hydrogenase.,Leroux F, Dementin S, Burlat B, Cournac L, Volbeda A, Champ S, Martin L, Guigliarelli B, Bertrand P, Fontecilla-Camps J, Rousset M, Leger C Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11188-93. Epub 2008 Aug 6. PMID:18685111<ref>PMID:18685111</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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The line below this paragraph, {{ABSTRACT_PUBMED_18685111}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3cus" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18685111 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18685111}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3CUS is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_fructosovorans Desulfovibrio fructosovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUS OCA].
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[[Category: Solidesulfovibrio fructosivorans]]
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[[Category: Volbeda A]]
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==Reference==
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<ref group="xtra">PMID:18685111</ref><ref group="xtra">PMID:9228943</ref><ref group="xtra">PMID:15803334</ref><references group="xtra"/>
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[[Category: Cytochrome-c3 hydrogenase]]
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[[Category: Desulfovibrio fructosovorans]]
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[[Category: Volbeda, A.]]
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[[Category: 3fe-4]]
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[[Category: 4fe-4]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Metal-binding]]
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[[Category: Ni-fe hydrogenase tunnel mutant]]
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[[Category: Nickel]]
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[[Category: Oxidoreductase]]
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[[Category: Periplasm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:28:43 2009''
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Current revision

Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution

PDB ID 3cus

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OCA

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