5xvk

Crystal structure of mouse Nicotinamide N-methyltransferase (NNMT) bound with end product, 1-methyl Nicotinamide (MNA)

spinqualitylabelsall models 5xvk, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xvk is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 8GC, GOL, SAH Activity: Nicotinamide N-methyltransferase, with EC number 2.1.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NNMT_MOUSE] Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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