3PZR
Crystals structure of aspartate beta-Semialdehyde dehydrogenase from Vibrio Cholerae with NADP and product of S-carbamoyl-L-cysteine
Summary for 3PZR
| Entry DOI | 10.2210/pdb3pzr/pdb |
| Related | 1MB4 3PWK 3PWS 3PYL 3PYX 3PZB 3Q0E 3Q11 3Q1L |
| Descriptor | Aspartate-semialdehyde dehydrogenase, CYSTEINE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | nadp, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 2 |
| Total formula weight | 82858.43 |
| Authors | Pavlovsky, A.G.,Potente, N.,Viola, R.E. (deposition date: 2010-12-14, release date: 2012-01-04, Last modification date: 2024-10-16) |
| Primary citation | Pavlovsky, A.G.,Liu, X.,Faehnle, C.R.,Potente, N.,Viola, R.E. Structural Characterization of Inhibitors with Selectivity against Members of a Homologous Enzyme Family. Chem.Biol.Drug Des., 79:128-136, 2012 Cited by PubMed Abstract: The aspartate biosynthetic pathway provides essential metabolites for many important biological functions, including the production of four essential amino acids. As this critical pathway is only present in plants and microbes, any disruptions will be fatal to these organisms. An early pathway enzyme, l-aspartate-β-semialdehyde dehydrogenase, produces a key intermediate at the first branch point of this pathway. Developing potent and selective inhibitors against several orthologs in the l-aspartate-β-semialdehyde dehydrogenase family can serve as lead compounds for antibiotic development. Kinetic studies of two small molecule fragment libraries have identified inhibitors that show good selectivity against l-aspartate-β-semialdehyde dehydrogenases from two different bacterial species, Streptococcus pneumoniae and Vibrio cholerae, despite the presence of an identical constellation of active site amino acids in this homologous enzyme family. Structural characterization of enzyme-inhibitor complexes have elucidated different modes of binding between these structurally related enzymes. This information provides the basis for a structure-guided approach to the development of more potent and more selective inhibitors. PubMed: 22039970DOI: 10.1111/j.1747-0285.2011.01267.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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