4EQ6 | pdb_00004eq6

The crystal structure of Psy3-Csm2 complex from budding yeast

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 
    0.228 (Depositor), 0.220 (DCC) 
  • R-Value Work: 
    0.201 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 
    0.201 (Depositor) 

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This is version 1.1 of the entry. See complete history. 


Literature

Structural and SAXS analysis of the budding yeast SHU-complex proteins

She, Z., Gao, Z.Q., Liu, Y., Wang, W.J., Liu, G.F., Shtykova, E.V., Xu, J.H., Dong, Y.H.

(2012) FEBS Lett 586: 2306-2312

  • DOI: https://doi.org/10.1016/j.febslet.2012.06.024
  • Primary Citation of Related Structures:  
    4EQ6

  • PubMed Abstract: 

    In Saccharomyces cerevisiae, four proteins, Shu1, Shu2, Psy3 and Csm2, form a stable SHU-complex both in vivo and in vitro. These proteins are involved in the early stages of the homologous recombination DNA damage repair process. In this paper, the crystal structure of the Psy3-Csm2 sub-complex is presented at 1.8Å resolution and successfully fitted into our small angle X-ray scattering (SAXS) data of the SHU-complex. Taken together with our electrophoretic mobility shift assay (EMSA) results, a model is proposed for the SHU-protein complex coupled with DNA.

    • Organizational Affiliation: 

    Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chromosome segregation in meiosis protein 2214Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: CSM2, YIL132C
UniProt
Find proteins for P40465 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P40465 
Go to UniProtKB:  P40465
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP40465
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Platinum sensitivity protein 3256Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: PSY3, YLR376C, L8039.17
UniProt
Find proteins for Q12318 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q12318 
Go to UniProtKB:  Q12318
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ12318
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free:  0.228 (Depositor), 0.220 (DCC) 
  • R-Value Work:  0.201 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 0.201 (Depositor) 
Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 135.333α = 90
b = 51.162β = 103.02
c = 77.049γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
SOLVEphasing
PHENIXrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-08-01
    Type: Initial release
  • Version 1.1: 2024-03-20
    Changes: Data collection, Database references