5MM8

Atomic resolution structure of SplE protease from Staphylococcus aureus

5MM8 の概要

• エントリーDOI: 10.2210/pdb5mm8/pdb
• 分子名称: Serine protease SplE, ACETATE ION (3 entities in total)
• 機能のキーワード: protease, staphylococcus aureus, virulence, hydrolase
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted : Q2FFT3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22246.13

構造登録者

Stach, N.,Zdzalik, M.,Dubin, G. (登録日: 2016-12-08, 公開日: 2018-03-28, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.75 Å)