1e5t
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT
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OverviewOverview
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.
About this StructureAbout this Structure
1E5T is a Single protein structure of sequence from Sus scrofa with GOL as ligand. Active as Prolyl oligopeptidase, with EC number 3.4.21.26 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612
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