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6h99

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Current revision (07:34, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6h99' size='340' side='right'caption='[[6h99]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='6h99' size='340' side='right'caption='[[6h99]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6h99]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H99 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6h99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobium_limicola_DSM_245 Chlorobium limicola DSM 245]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H99 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<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=6h99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h99 OCA], [http://pdbe.org/6h99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h99 RCSB], [http://www.ebi.ac.uk/pdbsum/6h99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h99 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6h99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h99 OCA], [https://pdbe.org/6h99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h99 RCSB], [https://www.ebi.ac.uk/pdbsum/6h99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h99 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B3ECE3_CHLL2 B3ECE3_CHLL2]
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Ergothioneine is an emergent factor in cellular redox biochemistry in humans and pathogenic bacteria. Broad consensus has formed around the idea that ergothioneine protects cells against reactive oxygen species. The recent discovery that anaerobic microorganisms make the same metabolite using oxygen-independent chemistry indicates that ergothioneine also plays physiological roles under anoxic conditions. In this report, we describe the crystal structure of the anaerobic ergothioneine biosynthetic enzyme EanB from green sulfur bacterium Chlorobium limicola. This enzyme catalyzes the oxidative sulfurization of N-alpha-trimethyl histidine. On the basis of structural and kinetic evidence, we describe the catalytic mechanism of this unusual C-S bond-forming reaction. Significant active-site conservation among distant EanB homologues suggests that the oxidative sulfurization of heterocyclic substrates may occur in a broad range of bacteria.
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Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis.,Leisinger F, Burn R, Meury M, Lukat P, Seebeck FP J Am Chem Soc. 2019 May 1;141(17):6906-6914. doi: 10.1021/jacs.8b12596. Epub 2019, Apr 23. PMID:30943021<ref>PMID:30943021</ref>
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==See Also==
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*[[Sulfurtransferase|Sulfurtransferase]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6h99" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chlorobium limicola DSM 245]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Burn, R]]
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[[Category: Burn R]]
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[[Category: Leisinger, F]]
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[[Category: Leisinger F]]
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[[Category: Lukat, P]]
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[[Category: Lukat P]]
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[[Category: Meury, M]]
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[[Category: Meury M]]
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[[Category: Seebeck, F P]]
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[[Category: Seebeck FP]]
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[[Category: Metabolic role: anaerobic ergothioneine biosynthesis chemical activity: sulfur transfer]]
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[[Category: Transferase]]
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Current revision

Crystal structure of anaerobic ergothioneine biosynthesis enzyme from Chlorobium limicola in persulfide form.

PDB ID 6h99

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