3ps7

Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa

spinqualitylabelsall models 3ps7, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ps7 is a 2 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PGO Related: 1dhp Gene: dapA (PSEAE) Activity: 4-hydroxy-tetrahydrodipicolinate synthase, with EC number 4.3.3.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DAPA_PSEAE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Publication Abstract from PubMed The intracellular enzyme dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) from Pseudomonas aeruginosa is a potential drug target because it is essential for the growth of bacteria while it is absent in humans. Therefore, in order to design new compounds using structure based approach for inhibiting the function of DHDPS from P. aeruginosa (Ps), we have cloned, characterized biochemically and biophysically and have determined its three-dimensional structure. The gene encoding DHDPS (dapA) was cloned in a vector pET-28c(+) and the recombinant protein was overexpressed in the Escherichia coli host. The K(m) values of the recombinant enzyme estimated for the substrates, pyruvate and (S)-aspartate-beta-semialdehyde [(S)-ASA] were found to be 0.90+/-0.13 mM and 0.17+/-0.02 mM, respectively. The circular dichroism studies showed that the enzyme adopts a characteristic beta/alpha conformation which is retained up to 65 degrees C. The fluorescence data indicated the presence of exposed tryptophan residues in the enzyme. The three-dimensional structure determination showed that DHDPS forms a homodimer which is stabilized by several hydrogen bonds and van der Waals forces at the interface. The active site formed with residues Thr44, Tyr107 and Tyr133 is found to be stereochemically suitable for catalytic function. It may be noted that Tyr107 of the catalytic triad belongs to the partner molecule in the dimer. The structure of the complex of PsDHDPS with (S)-lysine determined at 2.65 A resolution revealed the positions of three lysine molecules bound to the protein. Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa.,Kaur N, Gautam A, Kumar S, Singh A, Singh N, Sharma S, Sharma R, Tewari R, Singh TP Int J Biol Macromol. 2011 Jun 1;48(5):779-87. Epub 2011 Mar 10. PMID:21396954 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrodipicolinate synthase

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