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5XVK

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

Summary for 5XVK
Entry DOI10.2210/pdb5xvk/pdb
DescriptorNicotinamide N-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, 3-carbamoyl-1-methylpyridin-1-ium, ... (5 entities in total)
Functional Keywordsnnmt, mna, ternary complex, feedback inhibition, t2d, transferase
Biological sourceMus musculus (Mouse)
Total number of polymer chains2
Total formula weight64735.46
Authors
Swaminathan, S.,Birudukota, S.,Thakur, M.K.,Parveen, R.,Kandan, S.,Kannt, A.,Gosu, R. (deposition date: 2017-06-28, release date: 2017-08-02, Last modification date: 2023-11-22)
Primary citationSwaminathan, S.,Birudukota, S.,Thakur, M.K.,Parveen, R.,Kandan, S.,Juluri, S.,Shaik, S.,Anand, N.N.,Burri, R.R.,Kristam, R.,Hallur, M.S.,Rajagopal, S.,Schreuder, H.,Langer, T.,Rudolph, C.,Ruf, S.,Dhakshinamoorthy, S.,Gosu, R.,Kannt, A.
Crystal structures of monkey and mouse nicotinamide N-methyltransferase (NNMT) bound with end product, 1-methyl nicotinamide
Biochem. Biophys. Res. Commun., 491:416-422, 2017
Cited by
PubMed Abstract: 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 Å and 1.88 Å 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, α3) and long C-terminal loop. This might explain the mechanism of MNA acting as a feedback inhibitor of NNMT.
PubMed: 28720493
DOI: 10.1016/j.bbrc.2017.07.087
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.88 Å)
Structure validation

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