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Crystal Structure of Staphopain C from Staphylococcus aureus

ORCID
0000-0002-0445-5913
Affiliation
Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland;(M.M.);
Magoch, Malgorzata;
ORCID
0000-0003-4484-3512
Affiliation
CNRS, INSERM, Université de Strasbourg, IGBMC UMR 7104–UMR-S 1258, F-67400 Illkirch, France
McEwen, Alastair G.;
Affiliation
Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland;(M.M.);
Napolitano, Valeria;
ORCID
0000-0002-9075-3529
Affiliation
Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland
Władyka, Benedykt;
ORCID
0000-0002-5535-5760
Affiliation
Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland;(M.M.);
Dubin, Grzegorz

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.

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