View source for 5mgz


==Streptomyces Spheroides NovO (8-demethylnovbiocic acid methyltransferase) with SAH==
<StructureSection load='5mgz' size='340' side='right'caption='[[5mgz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_niveus Streptomyces niveus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MGZ 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5mgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mgz OCA], [https://pdbe.org/5mgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mgz RCSB], [https://www.ebi.ac.uk/pdbsum/5mgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mgz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOVO_STRNV NOVO_STRNV] C-methyltransferase that methylates 8-demethylnovobiocic acid to produce novobiocic acid in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.<ref>PMID:16274243</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
C-methylation of aromatic small molecules by C-methyltransferases (C-MTs) is an important biological transformation that involves C-C bond formation using S-adenosyl-l-methionine (SAM) as the methyl donor. Here, two advances in the mechanistic understanding of C-methylation of the 8-position of coumarin substrates catalyzed by the C-MT NovO from Streptomyces spheroides are described. First, a crystal structure of NovO reveals the Arg116-Asn117 and His120-Arg121 motifs are essential for coumarin substrate binding. Second, the active-site His120 is responsible for deprotonation of the phenolic 7-hydroxyl group on the coumarin substrate, activating the rate-determining methyl transfer step from SAM. This work expands our mechanistic knowledge of C-MTs, which could be used in the downstream development of engineered biocatalysts for small molecule C-alkylations.

Structural and Functional Basis of C-Methylation of Coumarin Scaffolds by NovO.,Sadler JC, Chung CH, Mosley JE, Burley GA, Humphreys LD ACS Chem Biol. 2017 Jan 13. doi: 10.1021/acschembio.6b01053. PMID:28068060<ref>PMID:28068060</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces niveus]]
[[Category: Chung C-W]]
[[Category: Mosley J]]
[[Category: Sadler JC]]