1QOJ

Crystal Structure of E.coli UvrB C-terminal domain, and a model for UvrB-UvrC interaction.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Observed: 0.327 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal Structure of E.Coli Uvrb C-Terminal Domain, and a Model for Uvrb-Uvrc Interaction

Sohi, M.Alexandrovich, A.Moolenaar, G.Visse, R.Goosen, N.Vernede, X.Fontecilla-Camps, J.Champness, J.Sanderson, M.R.

(2000) FEBS Lett 465: 161

  • DOI: https://doi.org/10.1016/s0014-5793(99)01690-7
  • Primary Citation of Related Structures:  
    1QOJ

  • PubMed Abstract: 

    A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices. From the UvrB' fold, a model for a domain of UvrC (UvrC') that has high sequence homology with UvrB' has been made. In the crystal, a dimerisation of UvrB domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning > 50 A.


  • Organizational Affiliation

    The Randall Institute, King's College, 26-29 Drury Lane, London, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UVRB
A, B
63Escherichia coliMutation(s): 3 
UniProt
Find proteins for P0A8F8 (Escherichia coli (strain K12))
Explore P0A8F8 
Go to UniProtKB:  P0A8F8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A8F8
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Observed: 0.327 
  • Space Group: P 62
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.81α = 90
b = 84.81β = 90
c = 53.19γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXL-97phasing
SOLVEphasing
SHELXL-97refinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-11-10
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-03-06
    Changes: Data collection, Derived calculations, Experimental preparation, Other