1E5T

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism

Fulop, V., Szeltner, Z., Polgar, L.

(2000) EMBO Rep 1: 277

  • DOI: https://doi.org/10.1093/embo-reports/kvd048
  • Primary Citation of Related Structures:  
    1E5T

  • PubMed Abstract: 

    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.

    • Organizational Affiliation: 

    Department of Biological Sciences, University of Warwick, Coventry, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROLYL ENDOPEPTIDASE710Sus scrofaMutation(s): 3 
EC: 3.4.21.26
UniProt
Find proteins for P23687 (Sus scrofa)
Explore P23687 
Go to UniProtKB:  P23687
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23687
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.7α = 90
b = 99.7β = 90
c = 110.9γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 2000-10-01 
    • Deposition Author(s): Fulop, V.

Revision History  (Full details and data files)

  • Version 1.0: 2000-10-01
    Type: Initial release
  • Version 1.1: 2011-08-31
    Changes: Data collection, Derived calculations, Non-polymer description, Other, Source and taxonomy, Structure summary, Version format compliance
  • Version 1.2: 2019-07-24
    Changes: Data collection, Derived calculations
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Refinement description