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Publication Abstract from PubMed

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.

Crystal Structure of Staphopain C from Staphylococcus aureus.,Magoch M, McEwen AG, Napolitano V, Wladyka B, Dubin G Molecules. 2023 May 29;28(11):4407. doi: 10.3390/molecules28114407. PMID:37298883^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.