4zfj
From Proteopedia
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| - | ''' | + | ==Ergothioneine-biosynthetic Ntn hydrolase EgtC, apo form== |
| + | <StructureSection load='4zfj' size='340' side='right' caption='[[4zfj]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zfj]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZFJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4zfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zfj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zfj RCSB], [http://www.ebi.ac.uk/pdbsum/4zfj PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EGTC_MYCS2 EGTC_MYCS2]] Catalyzes the hydrolysis of the gamma-glutamyl amide bond from N-(gamma-glutamyl)-[N(alpha),N(alpha),N(alpha)-trimethyl-L-histidinyl]-cysteine sulfoxide to produce hercynylcysteine sulfoxide.<ref>PMID:20420449</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nalpha-trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use gamma-glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of gamma-glutamyl cysteine is removed by the glutamine amidohydrolase EgtC and the beta-lyase EgtE. We determined the crystal structure of EgtC from Mycobacterium smegmatis in complex with its physiological substrate. The set of active site residues that define substrate specificity in EgtC are highly conserved, even in homologues that are not involved in ergothioneine production. This conservation is compounded by the phylogenetic distribution of EgtC-like enzymes indicates that their last common ancestor might have emerged for a purpose other than ergothioneine production. | ||
| - | + | Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.,Vit A, Mashabela GT, Blankenfeldt W, Seebeck FP Chembiochem. 2015 Jun 16. doi: 10.1002/cbic.201500168. PMID:26079795<ref>PMID:26079795</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Blankenfeldt, W]] | [[Category: Blankenfeldt, W]] | ||
| + | [[Category: Seebeck, F P]] | ||
[[Category: Vit, A]] | [[Category: Vit, A]] | ||
| + | [[Category: Ergothioneine biosynthesis]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Mycobacteria]] | ||
| + | [[Category: Ntn hydrolase]] | ||
| + | [[Category: Sulfur chemistry]] | ||
Revision as of 12:04, 1 July 2015
Ergothioneine-biosynthetic Ntn hydrolase EgtC, apo form
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