1GM5

Structure of RecG bound to three-way DNA junction

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.24 Å
  • R-Value Free: 0.328 
  • R-Value Work: 0.272 
  • R-Value Observed: 0.275 

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This is version 1.2 of the entry. See complete history. 


Literature

Structural Analysis of DNA Replication Fork Reversal by Recg

Singleton, M.R., Scaife, S., Wigley, D.B.

(2001) Cell 107: 79

  • DOI: https://doi.org/10.1016/s0092-8674(01)00501-3
  • Primary Citation of Related Structures:  
    1GM5

  • PubMed Abstract: 

    The stalling of DNA replication forks that occurs as a consequence of encountering DNA damage is a critical problem for cells. RecG protein is involved in the processing of stalled replication forks, and acts by reversing the fork past the damage to create a four-way junction that allows template switching and lesion bypass. We have determined the crystal structure of RecG bound to a DNA substrate that mimics a stalled replication fork. The structure not only reveals the elegant mechanism used by the protein to recognize junctions but has also trapped the protein in the initial stage of fork reversal. We propose a mechanism for how forks are processed by RecG to facilitate replication fork restart. In addition, this structure suggests that the mechanism and function of the two largest helicase superfamilies are distinct.

    • Organizational Affiliation: 

    ICRF Clare Hall Laboratories, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3LD, United Kingdom.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RECG780Thermotoga maritimaMutation(s): 0 
UniProt
Find proteins for Q9WY48 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
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Go to UniProtKB:  Q9WY48
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9WY48
Sequence Annotations
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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-(*CP*AP*GP*CP*TP*CP*CP*AP*TP*GP*AP*TP* CP*AP*TP*TP*GP*GP*CP*A)-3')B [auth X]20N/A
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Entity ID: 3
MoleculeChains LengthOrganismImage
DNA (5'-(*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*CP*AP* TP*GP*GP*AP*GP*CP*TP*G)-3')C [auth Y]20N/A
Sequence Annotations
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Entity ID: 4
MoleculeChains LengthOrganismImage
DNA (5'-(*GP*AP*GP*CP*AP*CP*TP*GP*C)-3')D [auth Z]9N/A
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ADP
Query on ADP
Download Ideal Coordinates CCD File 
E [auth A]ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
MG
Query on MG
Download Ideal Coordinates CCD File 
F [auth A]MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.24 Å
  • R-Value Free: 0.328 
  • R-Value Work: 0.272 
  • R-Value Observed: 0.275 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 133.704α = 90
b = 144.602β = 113.82
c = 84.023γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-10-03
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance