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| | <StructureSection load='6s7q' size='340' side='right'caption='[[6s7q]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='6s7q' size='340' side='right'caption='[[6s7q]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6s7q]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"spirillum_dentium"_(miller_1889)_sternberg_1892 "spirillum dentium" (miller 1889) sternberg 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S7Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s7q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola Treponema denticola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S7Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KZ5:(2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic+acid'>KZ5</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF9733_00339 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158 "Spirillum dentium" (Miller 1889) Sternberg 1892])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KZ5:(2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic+acid'>KZ5</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=6s7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s7q OCA], [http://pdbe.org/6s7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s7q RCSB], [http://www.ebi.ac.uk/pdbsum/6s7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s7q ProSAT]</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=6s7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s7q OCA], [https://pdbe.org/6s7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s7q RCSB], [https://www.ebi.ac.uk/pdbsum/6s7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s7q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/M2BPW8_TREDN M2BPW8_TREDN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leisinger, F]] | + | [[Category: Treponema denticola]] |
| - | [[Category: Seebeck, F P]] | + | [[Category: Leisinger F]] |
| - | [[Category: Ergothioneine]] | + | [[Category: Seebeck FP]] |
| - | [[Category: Ergothioneine degrading enzyme]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Tdetl]]
| + | |
| - | [[Category: Trimethlyammonium lyase]]
| + | |
| Structural highlights
Function
M2BPW8_TREDN
Publication Abstract from PubMed
Ergothioneine is a sulfur-containing histidine derivative that emerges from microbial biosynthesis and enters the human body through intestinal uptake and regulated distribution into specific tissues. Although the proteins involved in biosynthesis and uptake are well characterized, less is known about the degradative pathways of ergothioneine. This report describes the crystal structure of the active form of ergothionase from the oral pathogen Treponema denticola complexed with the substrate analogue desmethyl-ergothioneine sulfonic acid. This enzyme catalyzes the 1,2-elimination of trimethylamine from ergothioneine and ergothioneine sulfonic acid by using a unique mode of substrate activation combined with acid/base catalysis. This structural and mechanistic investigation revealed four essential catalytic residues, which are strictly conserved in homologous proteins from common gastrointestinal bacteria and numerous pathogenic bacteria, suggesting that bacterial activity may play an important role in determining the availability of ergothioneine in healthy and diseased human tissue.
Structure and Mechanism of Ergothionase from Treponema denticola.,Maurer A, Leisinger F, Lim D, Seebeck FP Chemistry. 2019 Jun 12. doi: 10.1002/chem.201901866. PMID:31188501[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maurer A, Leisinger F, Lim D, Seebeck FP. Structure and Mechanism of Ergothionase from Treponema denticola. Chemistry. 2019 Jun 12. doi: 10.1002/chem.201901866. PMID:31188501 doi:http://dx.doi.org/10.1002/chem.201901866
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