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EMBO Rep. 2000 Sep;1(3):277-81.

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.

Author information

1
Department of Biological Sciences, University of Warwick, Coventry, UK.

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.

PMID:
11256612
PMCID:
PMC1083722
DOI:
10.1093/embo-reports/kvd048
[Indexed for MEDLINE]
Free PMC Article

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