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1k4m
From Proteopedia
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Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD
Overview
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.
About this Structure
1K4M is a Single protein structure of sequence from Escherichia coli with NAD and CIT as ligands. Active as Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 18:51:32 2007
