1e5t | pdb_00001e5t
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| 1e5t, resolution 1.7Å | |||||||||||||
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| Sites: | AS and SS | ||||||||||||
| Ligands: | GOL | ||||||||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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