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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
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UNSPECIFIED. (2000) Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO REPORTS, 1 (3). pp. 277-281. ISSN 1469-221X
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Official URL: http://dx.doi.org/10.1093/embo-reports/kvd048
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.
| 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 |
| ISSN: | 1469-221X |
| Date: | September 2000 |
| Volume: | 1 |
| Number: | 3 |
| Number of Pages: | 5 |
| Page Range: | pp. 277-281 |
| Identification Number: | 10.1093/embo-reports/kvd048 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/12724 |
Data sourced from Thomson Reuters' Web of Knowledge
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