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[[Image:2e7z.png|left|200px]]
==Acetylene Hydratase from Pelobacter acetylenicus==
<StructureSection load='2e7z' size='340' side='right' caption='[[2e7z]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2e7z]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E7Z FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylenecarboxylate_hydratase Acetylenecarboxylate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.27 4.2.1.27] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2e7z RCSB], [http://www.ebi.ac.uk/pdbsum/2e7z PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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/initialview01.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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_2e7z|  PDB=2e7z  |  SCENE=  }}
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>


===Acetylene Hydratase from Pelobacter acetylenicus===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_17360611}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2e7z]] is a 1 chain structure with 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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:017360611</ref><ref group="xtra">PMID:016511024</ref><references group="xtra"/>
[[Category: Acetylenecarboxylate hydratase]]
[[Category: Acetylenecarboxylate hydratase]]
[[Category: Pelobacter acetylenicus]]
[[Category: Pelobacter acetylenicus]]

Revision as of 02:09, 30 September 2014

Acetylene Hydratase from Pelobacter acetylenicus

2e7z, resolution 1.26Å

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