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==EgtB from Chloracidobacterium thermophilum, a type II sulfoxide synthase in complex with N,N,N-trimethyl-histidine==
<StructureSection load='6qkj' size='340' side='right'caption='[[6qkj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qkj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chltf Chltf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QKJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVJ:N,N,N-TRIMETHYL-HISTIDINE'>AVJ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cabther_A1318 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=981222 CHLTF])</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=6qkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qkj OCA], [http://pdbe.org/6qkj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qkj RCSB], [http://www.ebi.ac.uk/pdbsum/6qkj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qkj ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sulfoxide synthases are nonheme iron enzymes that catalyze oxidative carbon-sulfur bond formation between cysteine derivatives and N-alpha-trimethylhistidine as a key step in the biosynthesis of thiohistidines. The complex catalytic mechanism of this enzyme reaction has emerged as the controversial subject of several biochemical and computational studies. These studies all used the structure of the gamma-glutamyl cysteine utilizing sulfoxide synthase, MthEgtB from Mycobacterium thermophilum (EC 1.14.99.50), as a structural basis. To provide an alternative model system, we have solved the crystal structure of CthEgtB from Chloracidobacterium thermophilum (EC 1.14.99.51) that utilizes cysteine as a sulfur donor. This structure reveals a completely different configuration of active site residues that are involved in oxygen binding and activation. Furthermore, comparison of the two EgtB structures enables a classification of all ergothioneine biosynthetic EgtBs into five subtypes, each characterized by unique active-site features. This active site diversity provides an excellent platform to examine the catalytic mechanism of sulfoxide synthases by comparative enzymology, but also raises the question as to why so many different solutions to the same biosynthetic problem have emerged.

An Alternative Active Site Architecture for O2 Activation in the Ergothioneine Biosynthetic EgtB from Chloracidobacterium thermophilum.,Stampfli AR, Goncharenko KV, Meury M, Dubey BN, Schirmer T, Seebeck FP J Am Chem Soc. 2019 Mar 18. doi: 10.1021/jacs.8b13023. PMID:30883103<ref>PMID:30883103</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qkj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chltf]]
[[Category: Large Structures]]
[[Category: Badri, B N]]
[[Category: Schirmer, T]]
[[Category: Seebeck, F P]]
[[Category: Stampfli, A R]]
[[Category: C-lectin]]
[[Category: Dinb]]
[[Category: Ergothioneine biosynthesis]]
[[Category: Oxidoreductase]]
[[Category: Sulfoxide synthase]]