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1e5t
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Proteases have a variety of strategies for selecting substrates in order | + | 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 Structure== | ==About this Structure== | ||
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[[Category: prolyl oligopeptidase]] | [[Category: prolyl oligopeptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:07 2008'' |
Revision as of 10:24, 21 February 2008
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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT
Overview
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 Structure
1E5T is a Single protein structure of sequence from Sus scrofa with 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.
Reference
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
Page seeded by OCA on Thu Feb 21 12:24:07 2008
