View source for 6zyl


==non-heme monooxygenase; ThoJ apo==
<StructureSection load='6zyl' size='340' side='right'caption='[[6zyl]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6zyl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_malaysiense Streptomyces malaysiense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZYL 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]] 2.09&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=6zyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zyl OCA], [https://pdbe.org/6zyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zyl RCSB], [https://www.ebi.ac.uk/pdbsum/6zyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zyl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1J4PXK4_9ACTN A0A1J4PXK4_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thioviridamide-like compounds, including thioholgamides, are ribosomally synthesized and post-translationally modified peptide natural products with potent anticancer cell activity and an unprecedented structure. Very little is known about their biosynthesis, and we were intrigued by the beta-hydroxy-N1, N3-dimethylhistidinium moiety found in these compounds. Here we report the construction of a heterologous host capable of producing thioholgamide with a 15-fold increased yield compared to the wild-type strain. A knockout of thoJ, encoding a predicted nonheme monooxygenase, shows that ThoJ is essential for thioholgamide beta-hydroxylation. The crystal structure of ThoJ exhibits a typical mono/dioxygenase fold with conserved key active-site residues. Yet, ThoJ possesses a very large substrate binding pocket that appears suitable to receive a cyclic thioholgamide intermediate for hydroxylation. The improved production of the heterologous host will enable the dissection of the individual biosynthetic steps involved in biosynthesis of this exciting RiPP family.

Non-Heme Monooxygenase ThoJ Catalyzes Thioholgamide beta-Hydroxylation.,Sikandar A, Lopatniuk M, Luzhetskyy A, Koehnke J ACS Chem Biol. 2020 Oct 1. doi: 10.1021/acschembio.0c00637. PMID:32965102<ref>PMID:32965102</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6zyl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces malaysiense]]
[[Category: Koehnke J]]
[[Category: Sikandar A]]