5m58: Difference between revisions
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==Crystal structure of CouO, a C-methyltransferase from Streptomyces rishiriensis== | |||
<StructureSection load='5m58' size='340' side='right' caption='[[5m58]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5m58]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M58 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m58 OCA], [http://pdbe.org/5m58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m58 RCSB], [http://www.ebi.ac.uk/pdbsum/5m58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m58 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5m58" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gruber, K]] | |||
[[Category: Pavkov-Keller, T]] | |||
[[Category: C-methyltransferase]] | |||
[[Category: Couo]] | |||
[[Category: Friedel-craft alkylation]] | |||
[[Category: Sam]] | |||
[[Category: Transferase]] | |||
[[Category: Transfrease]] | |||
