Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
UNSPECIFIED. (2000) Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO REPORTS, 1 (3). pp. 277-281. ISSN 1469-221XFull text not available from this repository.
Official URL: http://dx.doi.org/10.1093/embo-reports/kvd048
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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||EMBO REPORTS|
|Publisher:||OXFORD UNIV PRESS|
|Official Date:||September 2000|
|Number of Pages:||5|
|Page Range:||pp. 277-281|
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