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| | <StructureSection load='4chl' size='340' side='right'caption='[[4chl]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='4chl' size='340' side='right'caption='[[4chl]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4chl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4chl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chl OCA], [https://pdbe.org/4chl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chl RCSB], [https://www.ebi.ac.uk/pdbsum/4chl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chl ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.18 1.13.11.18] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chl OCA], [http://pdbe.org/4chl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4chl RCSB], [http://www.ebi.ac.uk/pdbsum/4chl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4chl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [[https://www.uniprot.org/uniprot/ETHE1_HUMAN ETHE1_HUMAN]] |
| - | The Ethylmalonic Encephalopathy Protein 1 (ETHE1) catalyzes the oxygen dependent oxidation of glutathione persulfide to give persulfite and glutathione. Mutations to the hETHE1 gene compromise sulfide metabolism leading to the genetic disease ethylmalonic encephalopathy. hETHE1 is a mono-iron binding member of the metallo-beta-lactamase fold superfamily. We report crystallographic analysis of hETHE1 in complex with iron to 2.6 A resolution. hETHE1 contains an alphabetabetaalpha MBL-fold, which supports metal-binding by the side-chains of an aspartate- and two histidine- residues; three water molecules complete an octahedral coordination of iron. The iron binding hETHE1 enzyme is related to the 'classical' di-zinc binding MBL hydrolases involved in antibiotic resistance, but has distinctive features. The two histidine-, and aspartate- residues involved in iron-binding in ETHE1, occupy similar positions to those observed by both the zinc 1 and zinc 2 binding sites in classical MBLs. The active site of hETHE1 is very similar to an ETHE1-like enzyme from Arabidopsis thaliana (60% sequence identity). A channel leading to the active site is sufficiently large to accommodate a glutathione persulfide substrate. Some of the observed hETHE1 clinical mutations cluster in the active site region. The structure will serve as a basis for detailed functional and mechanistic studies on ETHE1, and will be useful in the development of selective MBL inhibitors.
| + | |
| - | | + | |
| - | Crystal Structure of Human Persulfide Dioxygenase: Structural Basis of Ethylmalonic Encephalopathy.,Pettinati I, Brem J, McDonough MA, Schofield CJ Hum Mol Genet. 2015 Jan 16. pii: ddv007. PMID:25596185<ref>PMID:25596185</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4chl" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Brem J]] |
| - | [[Category: Brem, J]] | + | [[Category: McDonough MA]] |
| - | [[Category: McDonough, M A]] | + | [[Category: Pettinati I]] |
| - | [[Category: Pettinati, I]] | + | [[Category: Schofield CJ]] |
| - | [[Category: Schofield, C J]] | + | |
| - | [[Category: Glyoxalase ii family]]
| + | |
| - | [[Category: Sulfide detoxification]]
| + | |
