1n61

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[[Image:1n61.gif|left|200px]]
 
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==Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state==
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The line below this paragraph, containing "STRUCTURE_1n61", creates the "Structure Box" on the page.
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<StructureSection load='1n61' size='340' side='right'caption='[[1n61]], [[Resolution|resolution]] 1.30&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'>[[1n61]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Afipia_carboxidovorans_OM5 Afipia carboxidovorans OM5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N61 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]] 1.3&#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=CUN:CU(I)-S-MO(IV)(=O)OH+CLUSTER'>CUN</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1n61| PDB=1n61 | 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=1n61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n61 OCA], [https://pdbe.org/1n61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n61 RCSB], [https://www.ebi.ac.uk/pdbsum/1n61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n61 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCMS_AFIC5 DCMS_AFIC5] Catalyzes the oxidation of carbon monoxide to carbon dioxide.<ref>PMID:12475995</ref> <ref>PMID:21275368</ref>
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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/n6/1n61_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=1n61 ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state'''
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==See Also==
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*[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a 277-kDa Mo- and Cu-containing iron-sulfur flavoprotein. Here, the enzyme's active site in the oxidized or reduced state, after inactivation with potassium cyanide or with n-butylisocyanide bound to the active site, has been reinvestigated by multiple wavelength anomalous dispersion measurements at atomic resolution, electron spin resonance spectroscopy, and chemical analyses. We present evidence for a dinuclear heterometal [CuSMoO)OH] cluster in the active site of the oxidized or reduced enzyme, which is prone to cyanolysis. The cluster is coordinated through interactions of the Mo with the dithiolate pyran ring of molybdopterin cytosine dinucleotide and of the Cu with the Sgamma of Cys-388, which is part of the active-site loop VAYRC(388)SFR. The previously reported active-site structure [Dobbek, H., Gremer, L., Meyer, O. &amp; Huber, R. (1999) Proc. Natl. Acad. Sci. USA 96, 8884-8889] of an Mo with three oxygen ligands and an SeH-group bound to the Sgamma atom of Cys-388 could not be confirmed. The structure of CO dehydrogenase with the inhibitor n-butylisocyanide bound has led to a model for the catalytic mechanism of CO oxidation which involves a thiocarbonate-like intermediate state. The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Afipia carboxidovorans OM5]]
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1N61 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Oligotropha_carboxidovorans Oligotropha carboxidovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N61 OCA].
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[[Category: Large Structures]]
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[[Category: Dobbek H]]
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==Reference==
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[[Category: Gremer L]]
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Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution., Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O, Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15971-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12475995 12475995]
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[[Category: Huber R]]
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[[Category: Oligotropha carboxidovorans]]
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[[Category: Kiefersauer R]]
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[[Category: Protein complex]]
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[[Category: Meyer O]]
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[[Category: Dobbek, H.]]
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[[Category: Gremer, L.]]
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[[Category: Huber, R.]]
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[[Category: Kiefersauer, R.]]
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[[Category: Meyer, O.]]
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[[Category: Codh]]
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[[Category: Copper]]
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[[Category: Molybdenum]]
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[[Category: Molybdopterin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:08:17 2008''
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Current revision

Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state

PDB ID 1n61

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