2R0Q

Crystal structure of a serine recombinase- DNA regulatory complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.267 

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This is version 1.2 of the entry. See complete history


Literature

Architecture of a serine recombinase-DNA regulatory complex.

Mouw, K.W.Rowland, S.J.Gajjar, M.M.Boocock, M.R.Stark, W.M.Rice, P.A.

(2008) Mol Cell 30: 145-155

  • DOI: https://doi.org/10.1016/j.molcel.2008.02.023
  • Primary Citation of Related Structures:  
    2R0Q

  • PubMed Abstract: 

    An essential feature of many site-specific recombination systems is their ability to regulate the direction and topology of recombination. Resolvases from the serine recombinase family assemble an interwound synaptic complex that harnesses negative supercoiling to drive the forward reaction and promote recombination between properly oriented sites. To better understand the interplay of catalytic and regulatory functions within these synaptic complexes, we have solved the structure of the regulatory site synapse in the Sin resolvase system. It reveals an unexpected synaptic interface between helix-turn-helix DNA-binding domains that is also highlighted in a screen for synapsis mutants. The tetramer defined by this interface provides the foundation for a robust model of the synaptic complex, assembled entirely from available crystal structures, that gives insight into how the catalytic activity of Sin and other serine recombinases may be regulated.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Putative transposon Tn552 DNA-invertase bin3E [auth C],
F [auth D],
G [auth E],
H [auth F]
209Staphylococcus aureusMutation(s): 0 
Gene Names: bin3
UniProt
Find proteins for P20384 (Staphylococcus aureus)
Explore P20384 
Go to UniProtKB:  P20384
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP20384
Sequence Annotations
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  • Reference Sequence
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Entity ID: 1
MoleculeChains LengthOrganismImage
31-MERA,
C [auth G]
31N/A
Sequence Annotations
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains LengthOrganismImage
31-MERB,
D [auth H]
31N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.267 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 132.5α = 90
b = 132.5β = 90
c = 315.1γ = 120
Software Package:
Software NamePurpose
CNSrefinement
PDB_EXTRACTdata extraction
ADSCdata collection
HKL-3000data reduction
HKL-3000data scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-04-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations