Structure of the cupin protein GloB from Pseudomonas aeruginosa at 1.48 Å resolution

Pseudomonas aeruginosa is an opportunistic pathogen that causes severe infections in vulnerable patients. Highly virulent strains associated with hemorrhagic pneumonia harbor the glo nonribosomal peptide synthetase (NRPS) operon, the metabolic product of which remains unknown. The glo operon shares similarity with similar clusters from related bacteria, enabling the functional assignment of several glo genes, including gloB, which encodes a cupin-domain protein predicted to catalyze a metal-dependent step in the pathway. Here, we present the crystal structure of the GloB cupin domain from P. aeruginosa. The structure provides insight into part of the biosynthesis of an uncharacterized secondary metabolite and offers a foundation for understanding its potential contribution to bacterial pathogenicity.