1E5T

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

Summary for 1E5T

Entry DOI	10.2210/pdb1e5t/pdb
Related	1QFM 1QFS
Descriptor	PROLYL ENDOPEPTIDASE, GLYCEROL (3 entities in total)
Functional Keywords	hydrolase, prolyl oligopeptidase, amnesia, alpha/ beta-hydrolase, beta-propeller
Biological source	SUS SCROFA (PIG)
Total number of polymer chains	1
Total formula weight	81668.18
Authors	Fulop, V. (deposition date: 2000-08-02, release date: 2000-10-01, Last modification date: 2023-12-13)
Primary citation	Fulop, V.,Szeltner, Z.,Polgar, L. Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism Embo Rep., 1:277-, 2000 Cited by PubMed Abstract: 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. PubMed: 11256612 DOI: 10.1093/EMBO-REPORTS/KVD048 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation