1WXI
E.coli NAD Synthetase, AMP.PP
Summary for 1WXI
| Entry DOI | 10.2210/pdb1wxi/pdb |
| Related | 1WXE 1WXF 1WXG 1WXH |
| Descriptor | NH(3)-dependent NAD(+) synthetase, MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | nade, nad, e.coli, ligase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 31589.77 |
| Authors | Jauch, R.,Humm, A.,Huber, R.,Wahl, M.C. (deposition date: 2005-01-23, release date: 2005-02-15, Last modification date: 2024-03-13) |
| Primary citation | Jauch, R.,Humm, A.,Huber, R.,Wahl, M.C. Structures of Escherichia coli NAD Synthetase with Substrates and Products Reveal Mechanistic Rearrangements J.Biol.Chem., 280:15131-15140, 2005 Cited by PubMed Abstract: Nicotinamide adenine dinucleotide synthetases (NADS) catalyze the amidation of nicotinic acid adenine dinucleotide (NAAD) to yield the enzyme cofactor nicotinamide adenine dinucleotide (NAD). Here we describe the crystal structures of the ammonia-dependent homodimeric NADS from Escherichia coli alone and in complex with natural substrates and with the reaction product NAD. The structures disclosed two NAAD/NAD binding sites at the dimer interface and an adenosine triphosphate (ATP) binding site within each subunit. Comparison with the Bacillus subtilis NADS showed pronounced chemical differences in the NAAD/NAD binding sites and less prominent differences in the ATP binding pockets. In addition, the E. coli NADS structures revealed unexpected dynamical rearrangements in the NAAD/NAD binding pocket upon NAAD-to-NAD conversion, which define a catalysis state and a substrate/product exchange state. The two states are adopted by concerted movement of the nicotinysyl moieties of NAAD and NAD, Phe-170, and residues 224-228, which may be triggered by differential coordination of a magnesium ion to NAAD and NAD. Phylogenetic structure comparisons suggest that the present results are relevant for designing species-specific antibiotics. PubMed: 15699042DOI: 10.1074/jbc.M413195200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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