View source for 5xvq


==Crystal structure of monkey Nicotinamide N-methyltransferase (NNMT) bound with end product, 1-methyl Nicotinamide (MNA)==
<StructureSection load='5xvq' size='340' side='right' caption='[[5xvq]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xvq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XVQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8GC:1-methylpyridine-3-carboxamide'>8GC</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xvq OCA], [http://pdbe.org/5xvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xvq RCSB], [http://www.ebi.ac.uk/pdbsum/5xvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xvq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-l-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions. Here we report the first ternary complex X-ray crystal structures of monkey NNMT and mouse NNMT in bound form with the primary endogenous product, 1-methyl nicotinamide (MNA) and demethylated cofactor, S-adenosyl-homocysteine (SAH) determined at 2.30 A and 1.88 A respectively. The structural fold of these enzymes is identical to human NNMT. It is known that the primary endogenous product catalyzed by NNMT, MNA is a specific inhibitor of NNMT. Our data clearly indicates that the MNA binds to the active site and it would be trapped in the active site due to the formation of the bridge between the pole (long helix, alpha3) and long C-terminal loop. This might explain the mechanism of MNA acting as a feedback inhibitor of NNMT.

Crystal structures of monkey and mouse nicotinamide N-methyltransferase (NNMT) bound with end product, 1-methyl nicotinamide.,Swaminathan S, Birudukota S, Thakur MK, Parveen R, Kandan S, Juluri S, Shaik S, Anand NN, Burri RR, Kristam R, Hallur MS, Rajagopal S, Schreuder H, Langer T, Rudolph C, Ruf S, Dhakshinamoorthy S, Gosu R, Kannt A Biochem Biophys Res Commun. 2017 Jul 15. pii: S0006-291X(17)31437-7. doi:, 10.1016/j.bbrc.2017.07.087. PMID:28720493<ref>PMID:28720493</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xvq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Birudukota, S]]
[[Category: Gosu, R]]
[[Category: Kandan, S]]
[[Category: Kannt, A]]
[[Category: Parveen, R]]
[[Category: Swaminathan, S]]
[[Category: Thakur, M K]]
[[Category: Feedback inhibition]]
[[Category: Mna]]
[[Category: Nnmt]]
[[Category: T2d]]
[[Category: Ternary complex]]
[[Category: Transferase]]