PDBsum entry 2j04

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protein Protein-protein interface(s) links
Transcription PDB id
Protein chains
587 a.a. *
472 a.a. *
Waters ×5
* Residue conservation analysis
PDB id:
Name: Transcription
Title: The tau60-tau91 subcomplex of yeast transcription factor iiic
Structure: Hypothetical protein ypl007c. Chain: a, c. Synonym: tau60, ypl007p. Engineered: yes. Ydr362cp. Chain: b, d. Fragment: propeller domain, residues 159-672. Synonym: tau91. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
3.20Å     R-factor:   0.214     R-free:   0.257
Authors: A.Mylona,C.Fernandez-Tornero,P.Legrand,C.W.Muller
Key ref:
A.Mylona et al. (2006). Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly. Mol Cell, 24, 221-232. PubMed id: 17052456 DOI: 10.1016/j.molcel.2006.08.013
31-Jul-06     Release date:   23-Oct-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q12308  (TFC8_YEAST) -  Transcription factor tau 60 kDa subunit
588 a.a.
587 a.a.
Protein chains
Pfam   ArchSchema ?
Q06339  (TFC6_YEAST) -  Transcription factor tau 91 kDa subunit
672 a.a.
472 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   2 terms 
  Biological process     RNA polymerase III type 1 promoter transcriptional preinitiation complex assembly   8 terms 
  Biochemical function     RNA polymerase III type 1 promoter sequence-specific DNA binding     6 terms  


DOI no: 10.1016/j.molcel.2006.08.013 Mol Cell 24:221-232 (2006)
PubMed id: 17052456  
Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly.
A.Mylona, C.Fernández-Tornero, P.Legrand, M.Haupt, A.Sentenac, J.Acker, C.W.Müller.
Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the 3.2 A crystal structure of tau60 bound to a large C-terminal fragment of tau91 (Deltatau91). Deltatau91 protein contains a seven-bladed propeller preceded by an N-terminal extension, whereas tau60 contains a structurally homologous propeller followed by a C-terminal domain with a novel alpha/beta fold. The two propeller domains do not have any detectable DNA binding activity and mediate heterodimer formation that may serve as scaffold for tau138 assembly. We show that the C-terminal tau60 domain interacts with the TATA binding protein (TBP). Recombinant tauB recruits TBP and stimulates TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a combined contribution of tauA and tauB to preinitiation complex formation.
  Selected figure(s)  
Figure 1.
Figure 1. Crystal Structure of the Yeast τ60/Δτ91 Complex
(A) Ribbon representation of the τ60/Δτ91 complex. The N-terminal extension and the β propeller of Δτ91 are depicted in gold and blue, respectively. In τ60, β propeller and C-terminal domain are depicted in red and green, respectively. In Δτ91, the disordered loop BC in blade 1 and loop CD in blade 6 are depicted as dashed lines.
(B) Orthogonal view of the τ60/Δτ91 complex.
Figures 1, 2A, 2C, and 3A were generated with the program PyMOL (DeLano, 2002).
Figure 3.
Figure 3. The τ60/Δτ91 Interface
(A) Stereo diagram of the interactions between τ60 and Δτ91. The view corresponds to Figure 1A. Hydrogen bonds are indicated as dashed lines. Blades and strands involved in the interactions are indicated for both proteins.
(B) Summary of the interactions between τ60 and Δτ91. Strands, labeled from A to D, are represented by arrows. Hydrophobic, polar, basic, and acidic residues are in green, orange, blue, and red, respectively. Polar interactions involving main chain atoms are indicated as dashed gray lines, polar interactions between side chain atoms as gray lines, and hydrophobic interactions as green lines. The blades are labeled for both proteins.
(C) Conservation and electrostatic surface potentials of the τ60 and Δτ91 contact surfaces. The left and right panels show charge distribution (top) and sequence conservation (bottom) of the τ60 and Δτ91 contact surfaces, respectively. Sequence conservation above 70% is depicted in green based on a sequence alignment of different fungal orthologs (Figures S1 and S2). Dashed yellow lines indicate interacting regions. Regions of negative and positive surface potential are depicted in red and blue, respectively. Figures 3C and 4C were generated with the program GRASP (Nicholls et al., 1993).
  The above figures are reprinted by permission from Cell Press: Mol Cell (2006, 24, 221-232) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20451393 C.U.Stirnimann, E.Petsalaki, R.B.Russell, and C.W.Müller (2010).
WD40 proteins propel cellular networks.
  Trends Biochem Sci, 35, 565-574.  
17409385 H.Dumay-Odelot, C.Marck, S.Durrieu-Gaillard, O.Lefebvre, S.Jourdain, M.Prochazkova, A.Pflieger, and M.Teichmann (2007).
Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC.
  J Biol Chem, 282, 17179-17189.  
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