3QOE

Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.183 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.

Kim, Y.Joachimiak, G.Ye, Z.Binkowski, T.A.Zhang, R.Gornicki, P.Callahan, S.M.Hess, W.R.Haselkorn, R.Joachimiak, A.

(2011) Proc Natl Acad Sci U S A 108: 10109-10114

  • DOI: https://doi.org/10.1073/pnas.1106840108
  • Primary Citation of Related Structures:  
    3QOD, 3QOE

  • PubMed Abstract: 

    HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 Å. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and hood have no structural precedent in the protein database, therefore representing new folds. The structural assignments are supported by site-directed mutagenesis and DNA-binding studies. We suggest that HetR serves as a scaffold for assembly of transcription components critical for heterocyst development.


  • Organizational Affiliation

    Midwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, 9700 South Cass Avenue, Building 202, Argonne, IL 60439, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Heterocyst differentiation protein
A, B
302Fischerella thermalis PCC 7521Mutation(s): 0 
Gene Names: hetR
UniProt
Find proteins for Q2ACK9 (Fischerella thermalis PCC 7521)
Explore Q2ACK9 
Go to UniProtKB:  Q2ACK9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ2ACK9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.183 
  • Space Group: P 31
  • Diffraction Data: https://doi.org/10.18430/M33QOE
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 92.93α = 90
b = 92.93β = 90
c = 97.652γ = 120
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000data collection
HKL-3000phasing
MOLREPphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-20
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Refinement description