1CUK

ESCHERICHIA COLI RUVA PROTEIN AT PH 4.9 AND ROOM TEMPERATURE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction.

Rafferty, J.B.Sedelnikova, S.E.Hargreaves, D.Artymiuk, P.J.Baker, P.J.Sharples, G.J.Mahdi, A.A.Lloyd, R.G.Rice, D.W.

(1996) Science 274: 415-421

  • DOI: https://doi.org/10.1126/science.274.5286.415
  • Primary Citation of Related Structures:  
    1CUK

  • PubMed Abstract: 

    The Escherichia coli DNA binding protein RuvA acts in concert with the helicase RuvB to drive branch migration of Holliday intermediates during recombination and DNA repair. The atomic structure of RuvA was determined at a resolution of 1.9 angstroms. Four monomers of RuvA are related by fourfold symmetry in a manner reminiscent of a four-petaled flower. The four DNA duplex arms of a Holliday junction can be modeled in a square planar configuration and docked into grooves on the concave surface of the protein around a central pin that may facilitate strand separation during the migration reaction. The model presented reveals how a RuvAB-junction complex may also accommodate the resolvase RuvC.


  • Organizational Affiliation

    Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, UK. d.rice@sheffield.ac.uk


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RUVA PROTEIN203Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0A809 (Escherichia coli (strain K12))
Explore P0A809 
Go to UniProtKB:  P0A809
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A809
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.209 
  • Space Group: P 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.7α = 90
b = 83.7β = 90
c = 33.1γ = 90
Software Package:
Software NamePurpose
TNTrefinement
SDMSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-10-22
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Other