2GG6

CP4 EPSP synthase liganded with S3P


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.158 
  • R-Value Observed: 0.158 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Molecular basis for the herbicide resistance of Roundup Ready crops.

Funke, T.Han, H.Healy-Fried, M.L.Fischer, M.Schonbrunn, E.

(2006) Proc Natl Acad Sci U S A 103: 13010-13015

  • DOI: https://doi.org/10.1073/pnas.0603638103
  • Primary Citation of Related Structures:  
    2GG4, 2GG6, 2GGA, 2GGD

  • PubMed Abstract: 

    The engineering of transgenic crops resistant to the broad-spectrum herbicide glyphosate has greatly improved agricultural efficiency worldwide. Glyphosate-based herbicides, such as Roundup, target the shikimate pathway enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, the functionality of which is absolutely required for the survival of plants. Roundup Ready plants carry the gene coding for a glyphosate-insensitive form of this enzyme, obtained from Agrobacterium sp. strain CP4. Once incorporated into the plant genome, the gene product, CP4 EPSP synthase, confers crop resistance to glyphosate. Although widely used, the molecular basis for this glyphosate-resistance has remained obscure. We generated a synthetic gene coding for CP4 EPSP synthase and characterized the enzyme using kinetics and crystallography. The CP4 enzyme has unexpected kinetic and structural properties that render it unique among the known EPSP synthases. Glyphosate binds to the CP4 EPSP synthase in a condensed, noninhibitory conformation. Glyphosate sensitivity can be restored through a single-site mutation in the active site (Ala-100-Gly), allowing glyphosate to bind in its extended, inhibitory conformation.


  • Organizational Affiliation

    Department of Medicinal Chemistry, University of Kansas, Lawrence, 66045, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-phosphoshikimate 1-carboxyvinyltransferase455Agrobacterium sp. CP4Mutation(s): 0 
Gene Names: aroA
EC: 2.5.1.19
UniProt
Find proteins for Q9R4E4 (Agrobacterium sp. (strain CP4))
Explore Q9R4E4 
Go to UniProtKB:  Q9R4E4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9R4E4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.158 
  • R-Value Observed: 0.158 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.151α = 90
b = 44.861β = 106.32
c = 77.177γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
DENZOdata reduction
CNSrefinement
CrystalCleardata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-22
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description