1KFT

Solution Structure of the C-Terminal domain of UvrC from E-coli


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 22 
  • Selection Criteria: no NOE distance violations > 0.5A and lowest energies after refining the best 50 of the initial 200 in explicit water 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli

Singh, S.Folkers, G.E.Bonvin, A.M.J.J.Boelens, R.Wechselberger, R.Niztayev, A.Kaptein, R.

(2002) EMBO J 21: 6257-6266

  • DOI: https://doi.org/10.1093/emboj/cdf627
  • Primary Citation of Related Structures:  
    1KFT

  • PubMed Abstract: 

    The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' incision in the prokaryotic nucleotide excision repair process. We have determined the three-dimensional structure of the UvrC CTD using heteronuclear NMR techniques. The structure shows two helix-hairpin-helix (HhH) motifs connected by a small connector helix. The UvrC CTD is shown to mediate structure-specific DNA binding. The domain binds to a single-stranded-double-stranded junction DNA, with a strong specificity towards looped duplex DNA that contains at least six unpaired bases per loop ("bubble DNA"). Using chemical shift perturbation experiments, the DNA-binding surface is mapped to the first hairpin region encompassing the conserved glycine-valine-glycine residues followed by lysine-arginine-arginine, a positively charged surface patch and the second hairpin region consisting of glycine-isoleucine-serine. A model for the protein-DNA complex is proposed that accounts for this specificity.


  • Organizational Affiliation

    Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Excinuclease ABC subunit C78Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0A8G0 (Escherichia coli (strain K12))
Explore P0A8G0 
Go to UniProtKB:  P0A8G0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A8G0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 22 
  • Selection Criteria: no NOE distance violations > 0.5A and lowest energies after refining the best 50 of the initial 200 in explicit water 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-11-20
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations