3q1l

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently to Cys 128

spinqualitylabelsall models 3q1l, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q1l is a 4 chain structure with sequence from Streptococcus pneumoniae R6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: DHL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DQ00_STRR6 Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate (By similarity).[HAMAP-Rule:MF_02121] Publication Abstract from PubMed 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-beta-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-beta-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-beta-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. Structural Characterization of Inhibitors with Selectivity against Members of a Homologous Enzyme Family.,Pavlovsky AG, Liu X, Faehnle CR, Potente N, Viola RE Chem Biol Drug Des. 2012 Jan;79(1):128-36. doi:, 10.1111/j.1747-0285.2011.01267.x. Epub 2011 Nov 28. PMID:22039970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate-semialdehyde dehydrogenase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA