Image credit: Yujing Chen, Haizhu Jia, Jianyu Zhang, Yakun Liang, Ruihua Liu, Qionglin Zhang, and Mark Bartlam. Structure and mechanism of the γ-glutamyl-γ-aminobutyrate hydrolase SpuA from Pseudomonas aeruginosa. Acta Crystallographica Section D, Volume 77, Part 10, October 2021, Pages 1305-1316. DOI: 10.1107/S2059798321008986 Figure 1 (b)
Chen et al. reports that P. aeruginosa SpuA to be a member of the class I glutamine amidotransferase family with a preferential binding of γ-glutamyl-γ-aminobutyrate over glutamine in the IUCR Journal, Acta Crystallographica Section D, Volume 77, Part 10, Pages 1305-1316, published October 2021. SpuA, SpuA H221N, SpuA with γ-glu-GABA, and MsGATase crystals for structural determination were obtained by performing vapour diffusion experiements using the Crystal Screen Kit with 48-well sitting-drop plates.
The results of this research could potentially lead to new ways of dealing with multidrug resistant Pseudomonas aeruginosa infections.