3KYH

Saccharomyces cerevisiae Cet1-Ceg1 capping apparatus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.249 
  • R-Value Observed: 0.252 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the Saccharomyces cerevisiae Cet1-Ceg1 mRNA Capping Apparatus.

Gu, M.Rajashankar, K.R.Lima, C.D.

(2010) Structure 18: 216-227

  • DOI: https://doi.org/10.1016/j.str.2009.12.009
  • Primary Citation of Related Structures:  
    3KYH

  • PubMed Abstract: 

    The 5' guanine-N7 cap is the first cotranscriptional modification of messenger RNA. In Saccharomyces cerevisiae, the first two steps in capping are catalyzed by the RNA triphosphatase Cet1 and RNA guanylyltransferase Ceg1, which form a complex that is directly recruited to phosphorylated RNA polymerase II (RNAP IIo), primarily via contacts between RNAP IIo and Ceg1. A 3.0 A crystal structure of Cet1-Ceg1 revealed a 176 kDa heterotetrameric complex composed of one Cet1 homodimer that associates with two Ceg1 molecules via interactions between the Ceg1 oligonucleotide binding domain and an extended Cet1 WAQKW amino acid motif. The WAQKW motif is followed by a flexible linker that would allow Ceg1 to achieve conformational changes required for capping while maintaining interactions with both Cet1 and RNAP IIo. The impact of mutations as assessed through genetic analysis in S. cerevisiae is consonant with contacts observed in the Cet1-Ceg1 structure.


  • Organizational Affiliation

    Structural Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
mRNA-capping enzyme subunit beta
A, B
310Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: CET1P1433YPL228W
EC: 3.1.3.33
UniProt
Find proteins for O13297 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore O13297 
Go to UniProtKB:  O13297
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO13297
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
mRNA-capping enzyme subunit alpha
C, D
461Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: CEG1G2853YGL130W
EC: 2.7.7.50
UniProt
Find proteins for Q01159 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q01159 
Go to UniProtKB:  Q01159
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ01159
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.249 
  • R-Value Observed: 0.252 
  • Space Group: P 63
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 165.993α = 90
b = 165.993β = 90
c = 172.355γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
SOLOMONphasing
REFMACrefinement
PDB_EXTRACTdata extraction
MAR345dtbdata collection

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 2010-02-16 
  • Deposition Author(s): Lima, C.D.

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Author supporting evidence, Refinement description
  • Version 1.3: 2024-02-21
    Changes: Data collection, Database references, Refinement description