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[[Image:2e7z.jpg|left|200px]]


{{Structure
==Acetylene Hydratase from Pelobacter acetylenicus==
|PDB= 2e7z |SIZE=350|CAPTION= <scene name='initialview01'>2e7z</scene>, resolution 1.26&Aring;
<StructureSection load='2e7z' size='340' side='right'caption='[[2e7z]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene>
<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>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</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>
|GENE=
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7z OCA], [http://www.ebi.ac.uk/pdbsum/2e7z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e7z RCSB]</span>
== Function ==
}}
[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>
 
== Evolutionary Conservation ==
'''Acetylene Hydratase from Pelobacter acetylenicus'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/2e7z_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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.


==About this Structure==
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>
2E7Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pelobacter_acetylenicus Pelobacter acetylenicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Z OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/17360611 17360611]
[[Category: Deleted entry]]
[[Category: Pelobacter acetylenicus]]
[[Category: Single protein]]
[[Category: Einsle, O.]]
[[Category: Kroneck, P M.H.]]
[[Category: Messerschmidt, A.]]
[[Category: Seiffert, G B.]]
[[Category: dmso reductase family]]
[[Category: iron-sulfur-cluster]]
[[Category: tungstoprotein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:06 2008''
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2e7z" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Syntrophotalea acetylenica]]
[[Category: Einsle O]]
[[Category: Kroneck PMH]]
[[Category: Messerschmidt A]]
[[Category: Seiffert GB]]
Retrieved from "https://proteopedia.org/2e7z"