1LRI

BETA-CRYPTOGEIN-CHOLESTEROL COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.127 
  • R-Value Observed: 0.127 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

Lascombe, M.B.Ponchet, M.Venard, P.Milat, M.L.Blein, J.P.Prange, T.

(2002) Acta Crystallogr D Biol Crystallogr 58: 1442-1447

  • DOI: https://doi.org/10.1107/S0907444902011745
  • Primary Citation of Related Structures:  
    1LRI

  • PubMed Abstract: 

    Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.


  • Organizational Affiliation

    Laboratoire de Cristallographie et RMN Biologiques (UMR-8015, CNRS), Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75270 Paris CEDEX 06, France. lascombe@pharmacie.univ-paris5.fr


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-elicitin cryptogein98Phytophthora cryptogeaMutation(s): 0 
UniProt
Find proteins for P15570 (Phytophthora cryptogea)
Explore P15570 
Go to UniProtKB:  P15570
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15570
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.188 
  • R-Value Work: 0.127 
  • R-Value Observed: 0.127 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 30.964α = 90
b = 94.8β = 90
c = 65.296γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
SHELXL-97refinement
CCP4data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-05-29
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance