5MM8

Atomic resolution structure of SplE protease from Staphylococcus aureus

Summary for 5MM8

• Entry DOI: 10.2210/pdb5mm8/pdb
• Descriptor: Serine protease SplE, ACETATE ION (3 entities in total)
• Functional Keywords: protease, staphylococcus aureus, virulence, hydrolase
• Biological source: Staphylococcus aureus
• Cellular location: Secreted : Q2FFT3
• Total number of polymer chains: 1
• Total formula weight: 22246.13

Authors

Stach, N.,Zdzalik, M.,Dubin, G. (deposition date: 2016-12-08, release date: 2018-03-28, Last modification date: 2024-01-17)

Primary citation

Stach, N.,Kalinska, M.,Zdzalik, M.,Kitel, R.,Karim, A.,Serwin, K.,Rut, W.,Larsen, K.,Jabaiah, A.,Firlej, M.,Wladyka, B.,Daugherty, P.,Stennicke, H.,Drag, M.,Potempa, J.,Dubin, G.
Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus.
Structure, 26:572-579.e4, 2018

PubMed Abstract: Staphylococcus aureus is a dangerous human pathogen characterized by alarmingly increasing antibiotic resistance. Accumulating evidence suggests the role of Spl proteases in staphylococcal virulence. Spl proteases have restricted, non-overlapping substrate specificity, suggesting that they may constitute a first example of a proteolytic system in bacteria. SplA, SplB, and SplD were previously characterized in terms of substrate specificity and structural determinants thereof. Here we analyze the substrate specificity of SplE documenting its unique P1 preference among Spl proteases and, in fact, among all chymotrypsin-like (family S1) proteases characterized to date. This is interesting since our understanding of the general aspects of proteolysis is based on seminal studies of S1 family members. To better understand the molecular determinants of the unusual specificity of SplE, the crystal structure of the protein is determined here. Conclusions from structural analysis are evaluated by successful grafting of SplE specificity on the scaffold of SplB protease.

PubMed: 29526434
DOI: 10.1016/j.str.2018.02.008

Experimental method

X-RAY DIFFRACTION (1.75 Å)