Work

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

Year: 2026

Type: article

Abstract: 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.

Source: Acta Crystallographica Section F Structural Biology Communications

DOI: 10.1107/s2053230x26010514

Authors: Carlos Contreras-Martel, Kevin Duarte, Pauline Macheboeuf

Institutions: Centre National de la Recherche Scientifique, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Institut de Biologie Structurale

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Applied Microbiology and Biotechnology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green