3b53: Difference between revisions

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New page: left|200px<br /><applet load="3b53" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b53, resolution 1.500Å" /> '''Ni,Fe-CODH-320 mV s...
 
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[[Image:3b53.jpg|left|200px]]<br /><applet load="3b53" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3b53, resolution 1.500&Aring;" />
'''Ni,Fe-CODH-320 mV state'''<br />


==About this Structure==
==Ni,Fe-CODH-320 mV state==
3B53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=B51:'>B51</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B53 OCA].
<StructureSection load='3b53' size='340' side='right'caption='[[3b53]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
[[Category: Carbon-monoxide dehydrogenase (acceptor)]]
== Structural highlights ==
[[Category: Carboxydothermus hydrogenoformans]]
<table><tr><td colspan='2'>[[3b53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B53 FirstGlance]. <br>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
[[Category: Dobbek, H.]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
[[Category: Jeoung, J.H.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b53 OCA], [https://pdbe.org/3b53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b53 RCSB], [https://www.ebi.ac.uk/pdbsum/3b53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b53 ProSAT]</span></td></tr>
[[Category: B51]]
</table>
[[Category: FE2]]
== Function ==
[[Category: FES]]
[https://www.uniprot.org/uniprot/COOS2_CARHZ COOS2_CARHZ] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) (By similarity).
[[Category: SF4]]
== Evolutionary Conservation ==
[[Category: 4fe-4s]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: cluster c]]
Check<jmol>
[[Category: cytoplasm]]
  <jmolCheckbox>
[[Category: iron]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/3b53_consurf.spt"</scriptWhenChecked>
[[Category: iron-sulfur]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
[[Category: membrane]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: metal-binding]]
  </jmolCheckbox>
[[Category: nickel]]
</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=3b53 ConSurf].
[[Category: oxidoreductase]]
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C.


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:47:39 2008''
Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.,Jeoung JH, Dobbek H Science. 2007 Nov 30;318(5855):1461-4. PMID:18048691<ref>PMID:18048691</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3b53" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Carboxydothermus hydrogenoformans Z-2901]]
[[Category: Large Structures]]
[[Category: Dobbek H]]
[[Category: Jeoung JH]]

Latest revision as of 08:56, 13 August 2026

Ni,Fe-CODH-320 mV state

3b53, resolution 1.50Å

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