8OIG

Crystal Structure of Staphopain C from Staphylococcus aureus

Summary for 8OIG

Entry DOI	10.2210/pdb8oig/pdb
Descriptor	Thiol protease, GLYCEROL, CHLORIDE ION, ... (5 entities in total)
Functional Keywords	cystein protease, thiol protease, papain-fold, staphopain, hydrolase
Biological source	Staphylococcus aureus
Total number of polymer chains	3
Total formula weight	59461.13
Authors	McEwen, A.G.,Magoch, M.,Napolitano, V.,Dubin, G.,Wladyka, B. (deposition date: 2023-03-22, release date: 2023-06-21, Last modification date: 2024-06-19)
Primary citation	Magoch, M.,McEwen, A.G.,Napolitano, V.,Wladyka, B.,Dubin, G. Crystal Structure of Staphopain C from Staphylococcus aureus. Molecules, 28:-, 2023 Cited by PubMed Abstract: is a common opportunistic pathogen of humans and livestock that causes a wide variety of infections. The success of 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 , 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. PubMed: 37298883 DOI: 10.3390/molecules28114407 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.58 Å)

Structure validation