6zyl
From Proteopedia
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==non-heme monooxygenase; ThoJ apo== | ==non-heme monooxygenase; ThoJ apo== | ||
| - | <StructureSection load='6zyl' size='340' side='right'caption='[[6zyl]]' scene=''> | + | <StructureSection load='6zyl' size='340' side='right'caption='[[6zyl]], [[Resolution|resolution]] 2.09Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [ | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</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> | </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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces malaysiense]] | ||
[[Category: Koehnke J]] | [[Category: Koehnke J]] | ||
[[Category: Sikandar A]] | [[Category: Sikandar A]] | ||
Current revision
non-heme monooxygenase; ThoJ apo
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