2ADN

Solution structure of the bacterial antitoxin CcdA: Implications for DNA and toxin binding


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 

wwPDB Validation   3D Report Full Report

Currently 2ADN does not have a validation slider image.


This is version 1.3 of the entry. See complete history


Literature

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA

Madl, T.Van Melderen, L.Mine, N.Respondek, M.Oberer, M.Keller, W.Khatai, L.Zangger, K.

(2006) J Mol Biol 364: 170-185

  • DOI: https://doi.org/10.1016/j.jmb.2006.08.082
  • Primary Citation of Related Structures:  
    2ADL, 2ADN, 2H3A, 2H3C

  • PubMed Abstract: 

    Toxin-antitoxin systems are highly abundant in plasmids and bacterial chromosomes. They ensure plasmid maintenance by killing bacteria that have lost the plasmid. Their expression is autoregulated at the level of transcription. Here, we present the solution structure of CcdA, the antitoxin of the ccd system, as a free protein (16.7 kDa) and in complex with its cognate DNA (25.3 kDa). CcdA is composed of two distinct and independent domains: the N-terminal domain, responsible for DNA binding, which establishes a new family of the ribbon-helix-helix fold and the C-terminal region, which is responsible for the interaction with the toxin CcdB. The C-terminal domain is intrinsically unstructured and forms a tight complex with the toxin. We show that CcdA specifically recognizes a 6 bp palindromic DNA sequence within the operator-promoter (OP) region of the ccd operon and binds to DNA by insertion of the positively charged N-terminal beta-sheet into the major groove. The binding of up to three CcdA dimers to a 33mer DNA of its operator-promoter region was studied by NMR spectroscopy, isothermal titration calorimetry and single point mutation. The highly flexible C-terminal region of free CcdA explains its susceptibility to proteolysis by the Lon ATP-dependent protease.


  • Organizational Affiliation

    Institute of Chemistry, University of Graz, Graz 8010, Austria.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CcdA
A, B
72Escherichia coliMutation(s): 1 
UniProt
Find proteins for P62552 (Escherichia coli (strain K12))
Explore P62552 
Go to UniProtKB:  P62552
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP62552
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 

Structure Validation

View Full Validation Report

Currently 2ADN does not have a validation slider image.



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-22
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-10
    Changes: Database references, Derived calculations