View source for 2gcu


==X-Ray Structure of Gene Product from Arabidopsis Thaliana At1g53580==
<StructureSection load='2gcu' size='340' side='right'caption='[[2gcu]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gcu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GCU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g53580 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcu OCA], [https://pdbe.org/2gcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gcu RCSB], [https://www.ebi.ac.uk/pdbsum/2gcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gcu ProSAT], [https://www.topsan.org/Proteins/CESG/2gcu TOPSAN]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ETHE1_ARATH ETHE1_ARATH]] Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) gives rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. Required for normal endosperm development in seed, and thereby also required for normal embryo development.<ref>PMID:22786886</ref>  
== 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/gc/2gcu_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/main_output.php?pdb_ID=2gcu ConSurf].
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== Publication Abstract from PubMed ==
The protein product of gene At1g53580 from Arabidopsis thaliana possesses 54% sequence identity to a human enzyme that has been implicated in the rare disorder ethylmalonic encephalopathy. The structure of the At1g53580 protein has been solved to a nominal resolution of 1.48 Angstrom. This structure reveals tertiary structure differences between the ETHE1-like enzyme and glyoxalase II enzymes that are likely to account for differences in reaction chemistry and multimeric state between the two types of enzymes. In addition, the Arabidopsis ETHE1 protein is used as a model to explain the significance of several mutations in the human enzyme that have been observed in patients with ethylmalonic encephalopathy.

Structure of an ETHE1-like protein from Arabidopsis thaliana.,McCoy JG, Bingman CA, Bitto E, Holdorf MM, Makaroff CA, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):964-70. Epub 2006, Aug 19. PMID:16929096<ref>PMID:16929096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Hydrolase]]
[[Category: Large Structures]]
[[Category: Bingman, C A]]
[[Category: Bitto, E]]
[[Category: Structural genomic]]
[[Category: McCoy, J G]]
[[Category: Phillips, G N]]
[[Category: Wesenberg, G E]]
[[Category: Cesg]]
[[Category: Ethe1]]
[[Category: Ethylmalonic encephalopathy]]
[[Category: PSI, Protein structure initiative]]