1e5t

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{{STRUCTURE_1e5t| PDB=1e5t | SCENE= }}
{{STRUCTURE_1e5t| PDB=1e5t | SCENE= }}
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT'''
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===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 11256612 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:11:48 2008''

Revision as of 21:11, 30 June 2008

Image:1e5t.png

Template:STRUCTURE 1e5t

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

Template:ABSTRACT PUBMED 11256612

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 Tue Jul 1 00:11:48 2008

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