5A4N

Crystal structure of BPSL1147, a PC4 homolog from Burkholderia pseudomallei K96243 (tetragonal crystal form)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.214 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural Analysis and Knock-Out of a Burkholderia Pseudomallei Homolog of the Eukaryotic Transcription Coactivator Pc4.

Werten, S.Kohler, C.Bayer, N.Steinmetz, I.Hinrichs, W.

(2016) Gene 557: 140

  • DOI: https://doi.org/10.1016/j.gene.2015.11.037
  • Primary Citation of Related Structures:  
    5A4N, 5A4O

  • PubMed Abstract: 

    Homologs of the eukaryotic transcription coactivator PC4, which also functions in DNA repair and oxidative stress, were recently identified in prokaryotes. Crystallographic analysis of BPSL1147, a putative homolog from the pathogen Burkholderia pseudomallei K96243, reveals a highly conserved core structure and suggests a nucleic acid binding mode similar to that of PC4. Knock-out and complementation experiments do not reveal distinguishing phenotypes under normal growth conditions or in the presence of H2O2, arguing against a critical role in repair or the oxidative stress response of Burkholderia. These results may reflect redundancy or point at a bacteriophage origin of Burkholderia PC4 homologs.


  • Organizational Affiliation

    Department of Molecular Structural Biology, Institute for Biochemistry, University of Greifswald, Felix-Hausdorff-Strasse 4, D-17487 Greifswald, Germany. Electronic address: sebastiaan.werten@uni-greifswald.de.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BPSL1147
A, B
75Burkholderia pseudomallei K96243Mutation(s): 0 
UniProt
Find proteins for Q63VU8 (Burkholderia pseudomallei (strain K96243))
Explore Q63VU8 
Go to UniProtKB:  Q63VU8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ63VU8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.214 
  • Space Group: P 43 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.527α = 90
b = 56.527β = 90
c = 142.524γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-04-06
    Type: Initial release
  • Version 1.1: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description