1e5t: Difference between revisions
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT''' | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT''' | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
[[Category: | [[Category: Alpha/ beta-hydrolase]] | ||
[[Category: | [[Category: Amnesia]] | ||
[[Category: | [[Category: Beta-propeller]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Prolyl oligopeptidase]] | ||
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Revision as of 11:42, 2 May 2008
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. 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 Fri May 2 14:42:07 2008
