Title: Catalysis of serine oligopeptidases is controlled by a gating filter mechanism Fulop V, Szeltner Z, Polgar L Ref: EMBO Rep, 1:277, 2000 : PubMed
Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.
Representative scheme of S9N_PPCE_Peptidase_S9 structure and an image from PDBsum server
no Image
Databases
PDB-Sum
1E5T Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
1E5TFold classification based on Structure-Structure alignment of Proteins - FSSP server
