Crystal Structure of Staphopain C from Staphylococcus aureus

Malgorzata Magoch (1) , Alastair McEwen (2) , Valeria Napolitano (1) , Benedykt Władyka (1) , Grzegorz Dubin (1)

1 UJ - Uniwersytet Jagielloński w Krakowie = Jagiellonian University
2 IGBMC - Institut de Génétique et de Biologie Moléculaire et Cellulaire

Staphylococcus aureus is a common opportunistic pathogen of humans and livestock that causes a wide variety of infections. The success of S. aureus as a pathogen depends on the production of an array of virulence factors including cysteine proteases (staphopains)—major secreted proteases of certain strains of the bacterium. Here, we report the three-dimensional structure of staphopain C (ScpA2) of S. aureus, which shows the typical papain-like fold and uncovers a detailed molecular description of the active site. Because the protein is involved in the pathogenesis of a chicken disease, our work provides the foundation for inhibitor design and potential antimicrobial strategies against this pathogen.

Mots clés: ScpA2; Staphylococcus aureus; X-ray crystallography; cysteine protease; staphopain; virulence factor

Domaines: Biologie structurale [q-bio.BM]

Malgorzata Magoch, Alastair McEwen, Valeria Napolitano, Benedykt Władyka, Grzegorz Dubin. Crystal Structure of Staphopain C from Staphylococcus aureus. Molecules, 2023, 28 (11), pp.4407. ⟨10.3390/molecules28114407⟩. ⟨hal-04158826⟩