1GEF

Crystal structure of the archaeal holliday junction resolvase HJC

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.224 

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This is version 1.3 of the entry. See complete history. 


Literature

Crystal structure of the archaeal holliday junction resolvase Hjc and implications for DNA recognition.

Nishino, T., Komori, K., Tsuchiya, D., Ishino, Y., Morikawa, K.

(2001) Structure 9: 197-204

  • DOI: https://doi.org/10.1016/s0969-2126(01)00576-7
  • Primary Citation of Related Structures:  
    1GEF

  • PubMed Abstract: 

    Homologous recombination is a crucial mechanism in determining genetic diversity and repairing damaged chromosomes. Holliday junction is the universal DNA intermediate whose interaction with proteins is one of the major events in the recombinational process. Hjc is an archaeal endonuclease, which specifically resolves the junction DNA to produce two separate recombinant DNA duplexes. The atomic structure of Hjc should clarify the mechanisms of the specific recognition with Holliday junction and the catalytic reaction.

    • Organizational Affiliation: 

    Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HOLLIDAY JUNCTION RESOLVASEA,
B,
C [auth D],
D [auth E]		123Pyrococcus furiosusMutation(s): 0 
Gene Names: HJC
UniProt
Find proteins for E7FHX4 (Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1))
Explore E7FHX4 
Go to UniProtKB:  E7FHX4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupE7FHX4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.224 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 36.245α = 90
b = 119.056β = 90.66
c = 63.146γ = 90
Software Package:
Software NamePurpose
SHARPphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-03-21
    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: 2023-12-27
    Changes: Data collection, Database references, Derived calculations