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Title
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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
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Authors
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V.Fülöp,
Z.Szeltner,
L.Polgár.
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Ref.
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Embo Rep, 2000,
1,
277-281.
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PubMed id
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Abstract
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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.
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