Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity.

ABSTRACT: Intramembrane proteases hydrolyze peptide bonds within the cell membrane as the decision-making step of various signaling pathways. Sporulation factor IV B protease (SpoIVB) and C-terminal processing proteases B (CtpB) play central roles in cellular differentiation via regulated intramembrane proteolysis (RIP) process which activates pro-σ^K processing at the σ^K checkpoint during spore formation. SpoIVB joins CtpB in belonging to the widespread family of PDZ-proteases, but much remains unclear about the molecular mechanisms and structure of SpoIVB. In this study, we expressed inactive SpoIVB (SpoIVB^S378A) fused with maltose binding protein (MBP)-tag and obtained the solution structure of SpoIVB^S378A from its small angle X-ray scattering (SAXS) dat

SUBMITTER: Xie X 

PROVIDER: S-EPMC6581720 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature