6s7j - Revision history

OCA at 17:34, 14 August 2019

OCA — Wed, 14 Aug 2019 17:34:59 GMT

OCA: Protected "6s7j" [edit=sysop:move=sysop]

OCA — Wed, 17 Jul 2019 10:53:13 GMT

Protected "6s7j" [edit=sysop:move=sysop]

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Revision as of 10:53, 17 July 2019

OCA: New page: ==Native crystal structure of ergothioneine degrading enzyme Ergothionase from Treponema denticola== == Structural highlights ==
<table><tr><td colspan='2'>[[6s7j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S7J FirstGlance]. <br>
</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=6s7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s7j OCA], [http://pdbe.org/6s7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s7j RCSB], [http://www.ebi.ac.uk/pdbsum/6s7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s7j ProSAT]</span></td></tr>
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== 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<ref>PMID:31188501</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
TOC
</StructureSection>
[[Category: Large Structures]]
[[Category: Leisinger, F]]
[[Category: Seebeck, F P]]
[[Category: Ergothioneine]]
[[Category: Ergothioneine degrading enzyme]]
[[Category: Lyase]]
[[Category: Tdetl]]
[[Category: Trimethlyammonium lyase]]