3TIX

Crystal structure of the Chp1-Tas3 complex core


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS.

Schalch, T.Job, G.Shanker, S.Partridge, J.F.Joshua-Tor, L.

(2011) Nat Struct Mol Biol 18: 1351-1357

  • DOI: https://doi.org/10.1038/nsmb.2151
  • Primary Citation of Related Structures:  
    3TIX

  • PubMed Abstract: 

    RNA interference (RNAi) is critical for the assembly of heterochromatin at Schizosaccharomyces pombe centromeres. Central to this process is the RNA-induced initiation of transcriptional gene silencing (RITS) complex, which physically anchors small noncoding RNAs to chromatin. RITS includes Ago1, the chromodomain protein Chp1, and Tas3, which forms a bridge between Chp1 and Ago1. Chp1 is a large protein with no recognizable domains, apart from its chromodomain. Here we describe how the structured C-terminal half of Chp1 binds the Tas3 N-terminal domain, revealing the tight association of Chp1 and Tas3. The structure also shows a PIN domain at the C-terminal tip of Chp1 that controls subtelomeric transcripts through a post-transcriptional mechanism. We suggest that the Chp1-Tas3 complex provides a solid and versatile platform to recruit both RNAi-dependent and RNAi-independent gene-silencing pathways for locus-specific regulation of heterochromatin.


  • Organizational Affiliation

    Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ubiquitin-like protein SMT3,RNA-induced transcriptional silencing complex protein tas3
A, C
207Saccharomyces cerevisiae S288CSchizosaccharomyces pombe 972h-
This entity is chimeric
Mutation(s): 0 
Gene Names: SMT3YDR510WD9719.15tas3SPBC83.03c
UniProt
Find proteins for O94687 (Schizosaccharomyces pombe (strain 972 / ATCC 24843))
Explore O94687 
Go to UniProtKB:  O94687
Find proteins for Q12306 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q12306 
Go to UniProtKB:  Q12306
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsO94687Q12306
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Chromo domain-containing protein 1
B, D
458Schizosaccharomyces pombe 972h-Mutation(s): 0 
Gene Names: chp1SPAC18G6.02c
UniProt
Find proteins for Q10103 (Schizosaccharomyces pombe (strain 972 / ATCC 24843))
Explore Q10103 
Go to UniProtKB:  Q10103
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ10103
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
K
Query on K

Download Ideal Coordinates CCD File 
H [auth B],
J [auth C],
N [auth D]
POTASSIUM ION
K
NPYPAHLBTDXSSS-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
E [auth A]
F [auth A]
G [auth A]
I [auth B]
K [auth C]
E [auth A],
F [auth A],
G [auth A],
I [auth B],
K [auth C],
L [auth C],
M [auth D],
O [auth D]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.88α = 90
b = 172.2β = 90
c = 198.68γ = 90
Software Package:
Software NamePurpose
CBASSdata collection
HKL2Mapmodel building
SHELXmodel building
SHARPphasing
PHENIXrefinement
XDSdata reduction
XDSdata scaling
HKL2Mapphasing
SHELXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-16
    Type: Initial release
  • Version 1.1: 2011-12-07
    Changes: Database references
  • Version 1.2: 2011-12-21
    Changes: Database references
  • Version 1.3: 2017-06-07
    Changes: Database references
  • Version 1.4: 2017-11-08
    Changes: Refinement description
  • Version 1.5: 2024-02-28
    Changes: Data collection, Database references, Derived calculations