1e5t: Difference between revisions

Revision as of 13:24, 21 February 2008

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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OCA

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 ==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.
+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==
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 [[Category: prolyl oligopeptidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:37:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:07 2008''