Structural highlights
Publication Abstract from PubMedThe C5 pathway in bacteria is responsible for the synthesis of 5-aminolevulinic acid, which forms the core skeleton of cofactors required for metabolism. One of the key actors in this pathway is a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme called glutamate-1-semialdehyde aminomutase (GSAM). In this study, we crystallized the expression product of the uncharacterized pa4088 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1. The resulting high-resolution structure confirms it to be a member of the GSAM family. Continuous electron density indicates the presence of a PLP cofactor with a Schiff base linkage between the PLP cofactor and the epsilon-amino group of Lys286. A crystal structure of a K286A mutant in complex with PMP is also reported. As GSAM enzymes are not present in mammalian cells, this work provides a starting point for the investigation of GSAM as a target for drug development against P. aeruginosa infection. Crystal structure of a glutamate-1-semialdehyde-aminomutase from Pseudomonas aeruginosa PAO1.,Li S, Lou X, Xu Y, Teng X, Che S, Liu R, Bartlam M Biochem Biophys Res Commun. 2018 Jun 7;500(3):804-809. doi:, 10.1016/j.bbrc.2018.04.163. Epub 2018 Apr 24. PMID:29684343[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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