4b9b

The structure of the omega aminotransferase from Pseudomonas aeruginosa

spinqualitylabelsall models 4b9b, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b9b is a 8 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: CA, CL, GOL, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BAUA_PSEAE Involved in the degradation of beta-alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the presence of pyruvate as an amine acceptor. Publication Abstract from PubMed The crystal structures and inhibitor complexes of two industrially important omega-aminotransferase enzymes from Pseudomonas aeruginosa and Chromobacterium violaceum have been determined in order to understand the differences in their substrate specificity. The two enzymes share 30% sequence identity and use the same amino acceptor, pyruvate; however, the Pseudomonas enzyme shows activity towards the amino donor beta-alanine, whilst the Chromobacterium enzyme does not. Both enzymes show activity towards S-alpha-methylbenzylamine (MBA), with the Chromobacterium enzyme having a broader substrate range. The crystal structure of the P. aeruginosa enzyme has been solved in the holo form and with the inhibitor gabaculine bound. The C. violaceum enzyme has been solved in the apo and holo forms and with gabaculine bound. The structures of the holo forms of both enzymes are quite similar. There is little conformational difference observed between the inhibitor complex and the holoenzyme for the P. aeruginosa aminotransferase. In comparison, the crystal structure of the C. violaceum gabaculine complex shows significant structural rearrangements from the structures of both the apo and holo forms of the enzyme. It appears that the different rigidity of the protein scaffold contributes to the substrate specificity observed for the two omega-aminotransferases. Structural studies of Pseudomonas and Chromobacterium omega-aminotransferases provide insights into their differing substrate specificity.,Sayer C, Isupov MN, Westlake A, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):564-76. doi:, 10.1107/S0907444912051670. Epub 2013 Mar 14. PMID:23519665 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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