4KT5

Structure of GrlR-GrlA complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.185 

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This is version 1.2 of the entry. See complete history. 


Literature

Structure of GrlR-GrlA complex that prevents GrlA activation of virulence genes

Padavannil, A., Jobichen, C., Mills, E., Velazquez-Campoy, A., Li, M., Leung, K.Y., Mok, Y.K., Rosenshine, I., Sivaraman, J.

(2013) Nat Commun 4: 2546-2546

  • DOI: https://doi.org/10.1038/ncomms3546
  • Primary Citation of Related Structures:  
    4KT5

  • PubMed Abstract: 

    The locus of enterocyte effacement (LEE) is essential for virulence of enterohaemorrhagic Escherichia coli (EHEC) and enteropathogenic E. coli (EPEC). The 41 genes of the LEE encode type III secretion system proteins and three associated regulators: Ler, GrlA and GrlR. Ler is a positive regulator for most of the LEE operons, including grlRA. GrlA controls the expression of ler, ehxCABD and flhDC operons. GrlR binds to GrlA and suppresses its function. Here we report the crystal structure of GrlR-GrlAΔ (aa 1-106) complex (2:1) and its functional characterization. We show that GrlR interacts with the Helix-Turn-Helix motif of GrlA. Moreover, GrlA binds to the promoter DNA fragments of ler, ehxCABD and flhDC, and GrlR outcompetes with these promoter DNA sequences for the Helix-Turn-Helix motif of GrlA. These findings provide mechanistic insight into a regulatory module for the virulence of EPEC and EHEC, two important pathogens that cause devastating diseases.

    • Organizational Affiliation: 

    Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GrlR
A, B
127Escherichia coli O157:H7Mutation(s): 0 
Gene Names: grlR
UniProt
Find proteins for Q7DB61 (Escherichia coli O157:H7)
Explore Q7DB61 
Go to UniProtKB:  Q7DB61
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7DB61
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
GrlA137Escherichia coli O157:H7Mutation(s): 0 
Gene Names: grlA
UniProt
Find proteins for Q7DB62 (Escherichia coli O157:H7)
Explore Q7DB62 
Go to UniProtKB:  Q7DB62
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7DB62
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.185 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.188α = 90
b = 121.212β = 90
c = 84.831γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
PHENIXmodel building
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-10-09
    Type: Initial release
  • Version 1.1: 2013-10-16
    Changes: Database references
  • Version 1.2: 2018-02-21
    Changes: Experimental preparation