6a2f | pdb_00006a2f

Crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa

spinqualitylabelsall models 6a2f, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a2f is a 2 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: ACT, DLY, LLP, MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALR1_PSEAE Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. Publication Abstract from PubMed Alanine racemase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that reversibly catalyzes the conversion of l-alanine to d-alanine. d-alanine is an essential constituent in many prokaryotic cell structures. Inhibition of alanine racemase is lethal to prokaryotes, creating an attractive target for designing antibacterial drugs. Here we report the crystal structure of biosynthetic alanine racemase (Alr) from a pathogenic bacteria Pseudomonas aeruginosa PAO1. Structural studies showed that P. aeruginosa Alr (PaAlr) adopts a conserved homodimer structure. A guest substrate d-lysine was observed in the active site and refined to dual-conformation. Two buffer ions, malonate and acetate, were bound in the proximity to d-lysine. Biochemical characterization revealed the optimal reaction conditions for PaAlr. Enzymatic characterization and crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1.,Dong H, Han Q, Guo Y, Ju J, Wang S, Yuan C, Long W, He X, Xu S, Li S Biochem Biophys Res Commun. 2018 Sep 18;503(4):2319-2325. doi:, 10.1016/j.bbrc.2018.06.155. Epub 2018 Jun 30. PMID:29964014 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alanine racemase 3D structures

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