View source for 5m58


==Crystal structure of CouO, a C-methyltransferase from Streptomyces rishiriensis==
<StructureSection load='5m58' size='340' side='right'caption='[[5m58]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5m58]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rishiriensis Streptomyces rishiriensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M58 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=5m58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m58 OCA], [https://pdbe.org/5m58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m58 RCSB], [https://www.ebi.ac.uk/pdbsum/5m58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m58 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COUO_STRRH COUO_STRRH] Mediates C-methylation at the 8-position of the aminocoumarin moieties in coumermycin A1 in the biosynthetic pathway of coumermycin antibiotic. Active on both mono- and bis-amides for mono- and di-C-methylation adjacent to the phenolic hydroxyl before it is glycosylated by CouM.<ref>PMID:16274243</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Friedel-Crafts alkylation of aromatic systems is a classic reaction in organic chemistry, for which regiospecific mono-alkylation, however, is generally difficult to achieve. In nature, methyltransferases catalyze the addition of methyl groups to a wide range of biomolecules thereby modulating the physico-chemical properties of these compounds. Specifically, S-adenosyl-L-methionine dependent C-methyltransferases possess a high potential to serve as biocatalysts in environmentally benign organic syntheses. Here, we report on the high resolution crystal structure of CouO, a C-methyltransferase from Streptomyces rishiriensis involved in the biosynthesis of the antibiotic coumermycin A1. Through molecular docking calculations, site-directed mutagenesis and the comparison with homologous enzymes we identified His120 and Arg121 as key functional residues for the enzymatic activity of this group of C-methyltransferases. The elucidation of the atomic structure and the insight into the catalytic mechanism provide the basis for the (semi)-rational engineering of the enzyme in order to increase the substrate scope as well as to facilitate the acceptance of SAM-analogues as alternative cofactors.

Crystal Structure and Catalytic Mechanism of CouO, a Versatile C-Methyltransferase from Streptomyces rishiriensis.,Pavkov-Keller T, Steiner K, Faber M, Tengg M, Schwab H, Gruber-Khadjawi M, Gruber K PLoS One. 2017 Feb 2;12(2):e0171056. doi: 10.1371/journal.pone.0171056., eCollection 2017. PMID:28152088<ref>PMID:28152088</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5m58" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces rishiriensis]]
[[Category: Gruber K]]
[[Category: Pavkov-Keller T]]