2J5P

E. coli FtsK gamma domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: NO VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The Ftsk Gamma Domain Directs Oriented DNA Translocation by Interacting with Kops.

Sivanathan, V.Allen, M.D.De Bekker, C.Baker, R.Arciszewska, L.Freund, S.M.Bycroft, M.Lowe, J.Sherratt, D.J.

(2006) Nat Struct Mol Biol 13: 965

  • DOI: https://doi.org/10.1038/nsmb1158
  • Primary Citation of Related Structures:  
    2J5O, 2J5P

  • PubMed Abstract: 

    The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating completion of chromosome segregation. Translocase functions reside in three domains, alpha, beta and gamma. FtsKalphabeta are necessary and sufficient for ATP hydrolysis-dependent DNA translocation, which is modulated by FtsKgamma through its interaction with KOPS. By solving the FtsKgamma structure by NMR, we show that gamma is a winged-helix domain. NMR chemical shift mapping localizes the DNA-binding site on the gamma domain. Mutated proteins with substitutions in the FtsKgamma DNA-recognition helix are impaired in DNA binding and KOPS recognition, yet remain competent in DNA translocation and XerCD-dif site-specific recombination, which facilitates the late stages of chromosome segregation.


  • Organizational Affiliation

    Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA TRANSLOCASE FTSK76Escherichia coliMutation(s): 0 
UniProt
Find proteins for P46889 (Escherichia coli (strain K12))
Explore P46889 
Go to UniProtKB:  P46889
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46889
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: NO VIOLATIONS 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-04
    Type: Initial release
  • Version 1.1: 2017-04-19
    Changes: Other