2e7z

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(New page: 200px<br /><applet load="2e7z" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e7z, resolution 1.26&Aring;" /> '''Acetylene Hydratase ...)
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[[Image:2e7z.jpg|left|200px]]<br /><applet load="2e7z" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2e7z, resolution 1.26&Aring;" />
 
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'''Acetylene Hydratase from Pelobacter acetylenicus'''<br />
 
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==Overview==
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==Acetylene Hydratase from Pelobacter acetylenicus==
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The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its, class because it catalyzes a nonredox reaction, the hydration of acetylene, to acetaldehyde. Sequence comparisons group the protein into the dimethyl, sulfoxide reductase family, and it contains a bis-molybdopterin guanine, dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The, crystal structure of acetylene hydratase at 1.26 A now shows that the, tungsten center binds a water molecule that is activated by an adjacent, aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the, aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access, this previously unrecognized W-Asp active site, the protein evolved a new, substrate channel distant from where it is found in other molybdenum and, tungsten enzymes.
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<StructureSection load='2e7z' size='340' side='right'caption='[[2e7z]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2e7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Syntrophotalea_acetylenica Syntrophotalea acetylenica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E7Z 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]] 1.26&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</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=2e7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7z OCA], [https://pdbe.org/2e7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e7z RCSB], [https://www.ebi.ac.uk/pdbsum/2e7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e7z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AHY_SYNAC AHY_SYNAC] Catalyzes the hydration of acetylene to form acetaldehyde. Ethylene cannot act as a substrate.<ref>PMID:7592321</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/e7/2e7z_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=2e7z 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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The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.
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==About this Structure==
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Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.,Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3073-7. PMID:17360611<ref>PMID:17360611</ref>
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2E7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pelobacter_acetylenicus Pelobacter acetylenicus] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=W:'>W</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.71 4.2.1.71] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Z OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase., Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O, Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3073-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17360611 17360611]
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</div>
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[[Category: Deleted entry]]
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<div class="pdbe-citations 2e7z" style="background-color:#fffaf0;"></div>
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[[Category: Pelobacter acetylenicus]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Einsle, O.]]
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__TOC__
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[[Category: Kroneck, P.M.H.]]
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</StructureSection>
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[[Category: Messerschmidt, A.]]
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[[Category: Large Structures]]
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[[Category: Seiffert, G.B.]]
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[[Category: Syntrophotalea acetylenica]]
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[[Category: ACT]]
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[[Category: Einsle O]]
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[[Category: MGD]]
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[[Category: Kroneck PMH]]
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[[Category: MPD]]
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[[Category: Messerschmidt A]]
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[[Category: NA]]
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[[Category: Seiffert GB]]
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[[Category: SF4]]
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[[Category: W]]
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[[Category: dmso reductase family]]
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[[Category: iron-sulfur-cluster]]
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[[Category: tungstoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:17:10 2008''
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Current revision

Acetylene Hydratase from Pelobacter acetylenicus

PDB ID 2e7z

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