View source for 5thy


==Crystal structure of SeMet-Substituted CurJ carbon methyltransferase==
<StructureSection load='5thy' size='340' side='right'caption='[[5thy]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5thy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorena_producens_3L Moorena producens 3L]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5THY 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]] 2.087&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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=5thy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thy OCA], [https://pdbe.org/5thy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5thy RCSB], [https://www.ebi.ac.uk/pdbsum/5thy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5thy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F4Y426_9CYAN F4Y426_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Polyketide metabolites produced by modular type I polyketide synthases (PKS) acquire their chemical diversity through the variety of catalytic domains within modules of the pathway. Methyltransferases are among the least characterized of the catalytic domains common to PKS systems. We determined the domain boundaries and characterized the activity of a PKS C-methyltransferase (C-MT) from the curacin A biosynthetic pathway. The C-MT catalyzes S-adenosylmethionine-dependent methyl transfer to the alpha-position of beta-ketoacyl substrates linked to acyl carrier protein (ACP) or a small-molecule analog, but does not act on beta-hydroxyacyl substrates or malonyl-ACP. Key catalytic residues conserved in both bacterial and fungal PKS C-MTs were identified in a 2-A crystal structure and validated biochemically. Analysis of the structure and the sequences bordering the C-MT provides insight into the positioning of this domain within complete PKS modules.

Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.,Skiba MA, Sikkema AP, Fiers WD, Gerwick WH, Sherman DH, Aldrich CC, Smith JL ACS Chem Biol. 2016 Oct 10. PMID:27723289<ref>PMID:27723289</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5thy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Moorena producens 3L]]
[[Category: Skiba MA]]
[[Category: Smith JL]]