View source for 7uch


==AprA Methyltransferase 1 - GNAT in complex with Mn2+ , SAM, and Di-methyl-malonate==
<StructureSection load='7uch' size='340' side='right'caption='[[7uch]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7uch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorena_bouillonii Moorena bouillonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UCH 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]] 2.18&#8491;</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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MU6:dimethylpropanedioic+acid'>MU6</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=7uch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uch OCA], [https://pdbe.org/7uch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uch RCSB], [https://www.ebi.ac.uk/pdbsum/7uch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uch ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1U7N2Z8_9CYAN A0A1U7N2Z8_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Installation of methyl groups can significantly improve the binding of small-molecule drugs to protein targets; however, site-selective methylation often presents a significant synthetic challenge. Metal- and S-adenosyl-methionine (SAM)-dependent methyltransferases (MTs) in natural-product biosynthetic pathways are powerful enzymatic tools for selective or chemically challenging C-methylation reactions. Each of these MTs selectively catalyzes one or two methyl transfer reactions. Crystal structures and biochemical assays of the Mn(2+)-dependent monomethyltransferase from the saxitoxin biosynthetic pathway (SxtA MT) revealed the structural basis for control of methylation extent. The SxtA monomethyltransferase was converted to a dimethyltransferase by modification of the metal binding site, addition of an active site base, and an amino acid substitution to provide space in the substrate pocket for two methyl substituents. A reciprocal change converted a related dimethyltransferase into a monomethyltransferase, supporting our hypothesis that steric hindrance can prevent a second methylation event. A novel understanding of MTs will accelerate the development of MT-based catalysts and MT engineering for use in small-molecule synthesis.

Structural Basis for Control of Methylation Extent in Polyketide Synthase Metal-Dependent C-Methyltransferases.,Lao Y, Skiba MA, Chun SW, Narayan ARH, Smith JL ACS Chem Biol. 2022 Aug 19;17(8):2088-2098. doi: 10.1021/acschembio.2c00085. Epub, 2022 May 20. PMID:35594521<ref>PMID:35594521</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7uch" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Moorena bouillonii]]
[[Category: Lao Y]]
[[Category: Skiba MA]]
[[Category: Smith JL]]