3E27
Nicotinic acid mononucleotide (NaMN) adenylyltransferase from Bacillus anthracis: product complex
Summary for 3E27
| Entry DOI | 10.2210/pdb3e27/pdb |
| Descriptor | Nicotinate (Nicotinamide) nucleotide adenylyltransferase, NICOTINIC ACID ADENINE DINUCLEOTIDE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rossman-like fold, nucleotide-binding motif, nucleotidyltransferase, transferase |
| Biological source | Bacillus anthracis |
| Total number of polymer chains | 4 |
| Total formula weight | 90692.11 |
| Authors | Martynowski, D.,Eyobo, Y.,Zhang, H. (deposition date: 2008-08-05, release date: 2008-09-09, Last modification date: 2023-08-30) |
| Primary citation | Sorci, L.,Pan, Y.,Eyobo, Y.,Rodionova, I.,Huang, N.,Kurnasov, O.,Zhong, S.,MacKerell, A.D.,Zhang, H.,Osterman, A.L. Targeting NAD biosynthesis in bacterial pathogens: Structure-based development of inhibitors of nicotinate mononucleotide adenylyltransferase NadD. Chem.Biol., 16:849-861, 2009 Cited by PubMed Abstract: The emergence of multidrug-resistant pathogens necessitates the search for new antibiotics acting on previously unexplored targets. Nicotinate mononucleotide adenylyltransferase of the NadD family, an essential enzyme of NAD biosynthesis in most bacteria, was selected as a target for structure-based inhibitor development. Using iterative in silico and in vitro screens, we identified small molecule compounds that efficiently inhibited target enzymes from Escherichia coli (ecNadD) and Bacillus anthracis (baNadD) but had no effect on functionally equivalent human enzymes. On-target antibacterial activity was demonstrated for some of the selected inhibitors. A 3D structure of baNadD was solved in complex with one of these inhibitors (3_02), providing mechanistic insights and guidelines for further improvement. Most importantly, the results of this study help validate NadD as a target for the development of antibacterial agents with potential broad-spectrum activity. PubMed: 19716475DOI: 10.1016/j.chembiol.2009.07.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
