4zfk
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4zfk is ON HOLD until Paper Publication Authors: Vit, A., Seebeck, F.P., Blankenfeldt, W. Description: Ergothioneine-biosynthetic Ntn hydrolase Egt...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Ergothioneine-biosynthetic Ntn hydrolase EgtC with glutamine== | |
| + | <StructureSection load='4zfk' size='340' side='right'caption='[[4zfk]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zfk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZFK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82Å</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=GLN:GLUTAMINE'>GLN</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=4zfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zfk OCA], [https://pdbe.org/4zfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zfk RCSB], [https://www.ebi.ac.uk/pdbsum/4zfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zfk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4zfk" style="background-color:#fffaf0;"></div> |
| - | [[Category: Blankenfeldt | + | == References == |
| - | [[Category: Vit | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycolicibacterium smegmatis MC2 155]] | ||
| + | [[Category: Blankenfeldt W]] | ||
| + | [[Category: Seebeck FP]] | ||
| + | [[Category: Vit A]] | ||
Current revision
Ergothioneine-biosynthetic Ntn hydrolase EgtC with glutamine
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