2J49

Crystal structure of yeast TAF5 N-terminal domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.221 

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This is version 1.1 of the entry. See complete history


Literature

Crystal Structure, Biochemical and Genetic Characterization of Yeast and E. Cuniculi Taf(II)5 N-Terminal Domain: Implications for TFIID Assembly.

Romier, C.James, N.Birck, C.Cavarelli, J.Vivares, C.Collart, M.A.Moras, D.

(2007) J Mol Biol 368: 1292

  • DOI: https://doi.org/10.1016/j.jmb.2007.02.039
  • Primary Citation of Related Structures:  
    2J49, 2J4B

  • PubMed Abstract: 

    General transcription factor TFIID plays an essential role in transcription initiation by RNA polymerase II at numerous promoters. However, understanding of the assembly and a full structural characterization of this large 15 subunit complex is lacking. TFIID subunit TAF(II)5 has been shown to be present twice in this complex and to be critical for the function and assembly of TFIID. Especially, the TAF(II)5 N-terminal domain is required for its incorporation within TFIID and immuno-labelling experiments carried out by electron microscopy at low resolution have suggested that this domain might homodimerize, possibly explaining the three-lobed architecture of TFIID. However, the resolution at which the electron microscopy (EM) analyses were conducted is not sufficient to determine whether homodimerization occurs or whether a more intricate assembly implying other subunits is required. Here we report the X-ray structures of the fully evolutionary conserved C-terminal sub-domain of the TAF(II)5 N terminus, from yeast and the mammalian parasite Encephalitozoon cuniculi. This sub-domain displays a novel fold with specific surfaces having conserved physico-chemical properties that can form protein-protein interactions. Although a crystallographic dimer implying one of these surfaces is present in one of the crystal forms, several biochemical analyses show that this sub-domain is monomeric in solution, even at various salt conditions and in presence of different divalent cations. Consequently, the N-terminal sub-domain of the TAF(II)5 N terminus, which is homologous to a dimerization motif but has not been fully conserved during evolution, was studied by analytical ultracentrifugation and yeast genetics. Our results show that this sub-domain dimerizes at very high concentration but is neither required for yeast viability, nor for incorporation of two TAF(II)5 molecules within TFIID and for the assembly of this complex. Altogether, although our results do not argue in favour of a homodimerization of the TAF(II)5 N-terminal domain, our structural analyses suggest a role for this domain in assembly of TFIID and its related complexes SAGA, STAGA, TFTC and PCAF.


  • Organizational Affiliation

    Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Département de Biologie et Génomique Structurales, 1 rue Laurent Fries, B.P. 10142, 67404 Illkirch Cedex, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 5148Saccharomyces cerevisiaeMutation(s): 0 
UniProt
Find proteins for P38129 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38129 
Go to UniProtKB:  P38129
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38129
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.221 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 91.34α = 90
b = 91.34β = 90
c = 55.24γ = 120
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
SHARPphasing
SOLOMONphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-10
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance