8c9t: Difference between revisions

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-'''Unreleased structure'''
-The entry 8c9t is ON HOLD  until Paper Publication
+==Catechol O-methyltransferase from Streptomyces avermitilis==
+<StructureSection load='8c9t' size='340' side='right'caption='[[8c9t]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8c9t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avermitilis_MA-4680_=_NBRC_14893 Streptomyces avermitilis MA-4680 = NBRC 14893]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C9T FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8c9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c9t OCA], [https://pdbe.org/8c9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c9t RCSB], [https://www.ebi.ac.uk/pdbsum/8c9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c9t ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q82B68_STRAW Q82B68_STRAW]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Oxygen-directed methylation is a ubiquitous tailoring reaction in natural product pathways catalysed by O-methyltransferases (OMTs). Promiscuous OMT biocatalysts are thus a valuable asset in the toolkit for sustainable synthesis and optimization of known bioactive scaffolds for drug development. Here, we characterized the enzymatic properties and substrate scope of two bacterial OMTs from Desulforomonas acetoxidans and Streptomyces avermitilis and determined their crystal structures. Both OMTs methylated a wide range of catechol-like substrates, including flavonoids, coumarins, hydroxybenzoic acids, and their respective aldehydes, an anthraquinone and an indole. One enzyme also accepted a steroid. The product range included pharmaceutically relevant compounds such as (iso)fraxidin, iso(scopoletin), chrysoeriol, alizarin 1-methyl ether, and 2-methoxyestradiol. Interestingly, certain non-catechol flavonoids and hydroxybenzoic acids were also methylated. This study expands the knowledge on substrate preference and structural diversity of bacterial catechol OMTs and paves the way for their use in (combinatorial) pathway engineering.
-Authors: Zhang, L., Groves, M.R.
+Structural Characterization and Extended Substrate Scope Analysis of Two Mg(2+) -Dependent O-Methyltransferases from Bacteria.,Sokolova N, Zhang L, Deravi S, Oerlemans R, Groves MR, Haslinger K Chembiochem. 2023 Mar 21:e202300076. doi: 10.1002/cbic.202300076. PMID:36942619<ref>PMID:36942619</ref>
-Description: Catechol O-methyltransferase from Streptomyces avermitilis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Zhang, L]]
+<div class="pdbe-citations 8c9t" style="background-color:#fffaf0;"></div>
-[[Category: Groves, M.R]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptomyces avermitilis MA-4680 = NBRC 14893]]
+[[Category: Groves MR]]
+[[Category: Zhang L]]