4CPC

Crystal structure of human synaptonemal complex protein SYCP3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.24 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

A molecular model for the role of SYCP3 in meiotic chromosome organisation.

Syrjanen, J.L.Pellegrini, L.Davies, O.R.

(2014) Elife 3

  • DOI: https://doi.org/10.7554/eLife.02963
  • Primary Citation of Related Structures:  
    4CPC

  • PubMed Abstract: 

    The synaptonemal complex (SC) is an evolutionarily-conserved protein assembly that holds together homologous chromosomes during prophase of the first meiotic division. Whilst essential for meiosis and fertility, the molecular structure of the SC has proved resistant to elucidation. The SC protein SYCP3 has a crucial but poorly understood role in establishing the architecture of the meiotic chromosome. Here we show that human SYCP3 forms a highly-elongated helical tetramer of 20 nm length. N-terminal sequences extending from each end of the rod-like structure bind double-stranded DNA, enabling SYCP3 to link distant sites along the sister chromatid. We further find that SYCP3 self-assembles into regular filamentous structures that resemble the known morphology of the SC lateral element. Together, our data form the basis for a model in which SYCP3 binding and assembly on meiotic chromosomes leads to their organisation into compact structures compatible with recombination and crossover formation.


  • Organizational Affiliation

    Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SYNAPTONEMAL COMPLEX PROTEIN 3
A, B, C, D, E
A, B, C, D, E, F, G, H
167Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q8IZU3 (Homo sapiens)
Explore Q8IZU3 
Go to UniProtKB:  Q8IZU3
PHAROS:  Q8IZU3
GTEx:  ENSG00000139351 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8IZU3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.24 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 
  • Space Group: P 1
  • Diffraction Data: https://doi.org/10.18430/m34cpc
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.14α = 66.53
b = 92.381β = 82.32
c = 103.367γ = 76.53
Software Package:
Software NamePurpose
XDSdata reduction
Aimlessdata scaling
PHENIXphasing
BUSTER-TNTphasing
BUSTERrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-02
    Type: Initial release
  • Version 1.1: 2014-10-08
    Changes: Database references
  • Version 1.2: 2019-02-27
    Changes: Data collection, Database references, Other