1BEO

BETA-CRYPTOGEIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.218 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea, a member of a novel class of plant necrotic proteins.

Boissy, G.de La Fortelle, E.Kahn, R.Huet, J.C.Bricogne, G.Pernollet, J.C.Brunie, S.

(1996) Structure 4: 1429-1439

  • DOI: https://doi.org/10.1016/s0969-2126(96)00150-5
  • Primary Citation of Related Structures:  
    1BEO

  • PubMed Abstract: 

    Elicitins form a novel class of plant necrotic proteins which are secreted by Phytophthora and Pythium fungi, parasites of many economically important crops. These proteins induce leaf necrosis in infected plants and elicit an incompatible hypersensitive-like reaction, leading to the development of a systemic acquired resistance against a range of fungal and bacterial plant pathogens. No crystal structures of this class of protein are available. The crystal structure determination of beta-cryptogein (CRY), secreted by Phytophthora cryptogea, was undertaken to identify structural features important for the necrotic activity of elicitins.


  • Organizational Affiliation

    Unité de Recherche Biochimie & Structure des Protéines, INRA, Jouy-en-Josas, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BETA-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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.218 
  • Space Group: P 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.51α = 90
b = 46.51β = 90
c = 134.9γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SHARPphasing
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-05-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance