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| | <StructureSection load='6zyk' size='340' side='right'caption='[[6zyk]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='6zyk' size='340' side='right'caption='[[6zyk]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zyk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_malaysiense"_ser_et_al._2016 "streptomyces malaysiense" ser et al. 2016]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZYK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zyk]] 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=6ZYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZYK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VT52_024865 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1428626 "Streptomyces malaysiense" Ser et al. 2016])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <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'>[http://proteopedia.org/fgij/fg.htm?mol=6zyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zyk OCA], [http://pdbe.org/6zyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zyk RCSB], [http://www.ebi.ac.uk/pdbsum/6zyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zyk ProSAT]</span></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=6zyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zyk OCA], [https://pdbe.org/6zyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zyk RCSB], [https://www.ebi.ac.uk/pdbsum/6zyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zyk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1J4PXK4_9ACTN A0A1J4PXK4_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces malaysiense ser et al. 2016]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Koehnke, J]] | + | [[Category: Streptomyces malaysiense]] |
| - | [[Category: Sikandar, A]] | + | [[Category: Koehnke J]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Sikandar A]] |
| - | [[Category: Non-heme monooxygenase]]
| + | |
| Structural highlights
Function
A0A1J4PXK4_9ACTN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sikandar A, Lopatniuk M, Luzhetskyy A, Koehnke J. Non-Heme Monooxygenase ThoJ Catalyzes Thioholgamide beta-Hydroxylation. ACS Chem Biol. 2020 Oct 1. doi: 10.1021/acschembio.0c00637. PMID:32965102 doi:http://dx.doi.org/10.1021/acschembio.0c00637
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