1GXQ

Crystal structure of the PhoB effector domain

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


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


Literature

Tandem DNA Recognition by Two-Component Signal Transduction Transcriptional Activator Phob

Blanco, A.G., Sola, M., Gomis-Ruth, F.X., Coll, M.

(2002) Structure 10: 701

  • DOI: https://doi.org/10.1016/s0969-2126(02)00761-x
  • Primary Citation of Related Structures:  
    1GXP, 1GXQ

  • PubMed Abstract: 

    PhoB is a signal transduction response regulator that activates nearly 40 genes in phosphate depletion conditions in E. coli and closely related bacteria. The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix. The protein has a winged helix fold in which the DNA recognition elements comprise helix alpha 3, penetrating the major groove, and a beta hairpin wing interacting with a compressed minor groove via Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation loops protrude laterally in an appropriate orientation to interact with the RNA polymerase sigma(70) subunit, which triggers transcription initiation.

    • Organizational Affiliation: 

    Institut de Biologia Molecular de Barcelona, CSIC, Jordi Girona, 18-26, E-08034 Barcelona, Spain.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHATE REGULON TRANSCRIPTIONAL REGULATORY PROTEIN PHOB106Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0AFJ5 (Escherichia coli (strain K12))
Explore P0AFJ5 
Go to UniProtKB:  P0AFJ5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AFJ5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.200 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.65α = 90
b = 37.29β = 90
c = 30.51γ = 90
Software Package:
Software NamePurpose
CNSrefinement
MOSFLMdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-04-29
    Type: Initial release
  • Version 1.1: 2015-02-25
    Changes: Database references, Derived calculations, Non-polymer description, Other, Refinement description, Source and taxonomy, Structure summary, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Refinement description