3hfj | pdb_00003hfj

Bacillus anthracis nicotinate mononucleotide adenylytransferase (nadD) in complex with inhibitor CID 3289443

spinqualitylabelsall models 3hfj, resolution 2.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hfj is a 2 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, DZ9 Gene: BAS4230, NadD ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q6HT60_BACAN] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).[HAMAP-Rule:MF_00244] 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 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. Targeting NAD biosynthesis in bacterial pathogens: Structure-based development of inhibitors of nicotinate mononucleotide adenylyltransferase NadD.,Sorci L, Pan Y, Eyobo Y, Rodionova I, Huang N, Kurnasov O, Zhong S, MacKerell AD Jr, Zhang H, Osterman AL Chem Biol. 2009 Aug 28;16(8):849-61. PMID:19716475 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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