1e5t: Difference between revisions

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{{STRUCTURE_1e5t|  PDB=1e5t  |  SCENE=  }}  
{{STRUCTURE_1e5t|  PDB=1e5t  |  SCENE=  }}  


'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT'''
===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT===




==Overview==
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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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{{ABSTRACT_PUBMED_11256612}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Prolyl oligopeptidase]]
[[Category: Prolyl oligopeptidase]]
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