6SF7

Atomic resolution structure of SplF protease from Staphylococcus aureus

Summary for 6SF7

• Entry DOI: 10.2210/pdb6sf7/pdb
• Descriptor: Serine protease SplF, DI(HYDROXYETHYL)ETHER, SULFATE ION, ... (6 entities in total)
• Functional Keywords: virulence factor, protease, bacterial, hydrolase
• Biological source: Staphylococcus aureus subsp. aureus USA300
• Total number of polymer chains: 4
• Total formula weight: 90014.34

Authors

Golik, P.,Stach, N.,Karim, A.,Dubin, G. (deposition date: 2019-08-01, release date: 2021-03-03, Last modification date: 2024-05-15)

Primary citation

Stach, N.,Karim, A.,Golik, P.,Kitel, R.,Pustelny, K.,Gruba, N.,Groborz, K.,Jankowska, U.,Kedracka-Krok, S.,Wladyka, B.,Drag, M.,Lesner, A.,Dubin, G.
Structural Determinants of Substrate Specificity of SplF Protease from Staphylococcus aureus .
Int J Mol Sci, 22:-, 2021

PubMed Abstract: Accumulating evidence suggests that six proteases encoded in the operon of a dangerous human pathogen, , may play a role in virulence. Interestingly, SplA, B, D, and E have complementary substrate specificities while SplF remains to be characterized in this regard. Here, we describe the prerequisites of a heterologous expression system for active SplF protease and characterize the enzyme in terms of substrate specificity and its structural determinants. Substrate specificity of SplF is comprehensively profiled using combinatorial libraries of peptide substrates demonstrating strict preference for long aliphatic sidechains at the P1 subsite and significant selectivity for aromatic residues at P3. The crystal structure of SplF was provided at 1.7 Å resolution to define the structural basis of substrate specificity of SplF. The obtained results were compared and contrasted with the characteristics of other Spl proteases determined to date to conclude that the operon encodes a unique extracellular proteolytic system.

PubMed: 33672341
DOI: 10.3390/ijms22042220

Experimental method

X-RAY DIFFRACTION (1.7 Å)