1k4m | pdb_00001k4m

Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD

spinqualitylabelsall models 1k4m, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k4m is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CIT, NAD Related: 1k4k Gene: NADD ("Bacillus coli" Migula 1895) Activity: Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NADD_ECOLI] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria inhibitors. The crystal structures of E. coli NaMN adenylyltransferase (NMNAT) and its complex with deamido-NAD (NaAD) revealed that ligand binding causes large conformational changes in several loop regions around the active site. The enzyme specifically recognizes the deamidated pyridine nucleotide through interactions between nicotinate carboxylate with several protein main chain amides and a positive helix dipole. Comparison of E. coli NMNAT with those from archaeal organisms revealed extensive differences in the active site architecture, enzyme-ligand interaction mode, and bound dinucleotide conformations. The bacterial NaMN adenylyltransferase structures described here provide a foundation for structure-based design of specific inhibitors that may have therapeutic potential. Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.,Zhang H, Zhou T, Kurnasov O, Cheek S, Grishin NV, Osterman A Structure. 2002 Jan;10(1):69-79. PMID:11796112 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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