2O97

Crystal Structure of E. coli HU heterodimer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.228 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Spiral structure of Escherichia coli HU{alpha}beta provides foundation for DNA supercoiling.

Guo, F.Adhya, S.

(2007) Proc Natl Acad Sci U S A 104: 4309-4314

  • DOI: https://doi.org/10.1073/pnas.0611686104
  • Primary Citation of Related Structures:  
    2O97

  • PubMed Abstract: 

    We determined the crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein by x-ray diffraction and observed that the heterodimers form multimers with octameric units in three potential arrangements, which may serve specialized roles in different DNA transaction reactions. It is of special importance that one of the structures forms spiral filaments with left-handed rotations. A negatively superhelical DNA can be modeled to wrap around this left-handed HUalphabeta multimer. Whereas the wild-type HU generated negative DNA supercoiling in vitro, an engineered heterodimer with an altered amino acid residue critical for the formation of the left-handed spiral protein in the crystal was defective in the process, thus providing the structural explanation for the classical property of HU to restrain negative supercoils in DNA.


  • Organizational Affiliation

    Laboratory of Molecular Biology, National Cancer Institute, 37 Convent Drive, Bethesda, MD 20892-4264, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-binding protein HU-alpha90Escherichia coliMutation(s): 0 
Gene Names: hupA
UniProt
Find proteins for P0ACF0 (Escherichia coli (strain K12))
Explore P0ACF0 
Go to UniProtKB:  P0ACF0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0ACF0
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-binding protein HU-beta90Escherichia coliMutation(s): 0 
Gene Names: hupBhopD
UniProt
Find proteins for P0ACF4 (Escherichia coli (strain K12))
Explore P0ACF4 
Go to UniProtKB:  P0ACF4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0ACF4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.228 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 82.915α = 90
b = 82.915β = 90
c = 61.048γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
DMphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-03-06
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references, Derived calculations