8qfo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Ergothioneine dioxygenase, variant Y128F, from Thermocatellispora tengchongensis in complex with manganese== | |
| + | <StructureSection load='8qfo' size='340' side='right'caption='[[8qfo]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8qfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QFO 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]] 2.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8qfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qfo OCA], [https://pdbe.org/8qfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qfo RCSB], [https://www.ebi.ac.uk/pdbsum/8qfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qfo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A840P3H4_9ACTN A0A840P3H4_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ergothioneine is a sulfur-containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants including singlet oxygen or hydrogen peroxide, and may therefore protect cells against oxidative stress. In this report we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron-dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal-dependent ergothioneine sulfinic acid desulfinase that produces Na-trimethylhistidine and SO2. The discovery that certain actinobacteria contain the enzymatic machinery for O2-dependent biosynthesis and O2-dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content. | ||
| - | + | Enzyme-Catalyzed Oxidative Degradation of Ergothioneine.,Nalivaiko E, Vasseur CM, Seebeck FP Angew Chem Int Ed Engl. 2023 Dec 14:e202318445. doi: 10.1002/anie.202318445. PMID:38095354<ref>PMID:38095354</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8qfo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Seebeck FP]] | ||
| + | [[Category: Vasseur CM]] | ||
Revision as of 23:14, 27 December 2023
Ergothioneine dioxygenase, variant Y128F, from Thermocatellispora tengchongensis in complex with manganese
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