1NVP

HUMAN TFIIA/TBP/DNA COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.229 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Novel interactions between the components of human and yeast TFIIA/TBP/DNA complexes.

Bleichenbacher, M.Tan, S.Richmond, T.J.

(2003) J Mol Biol 332: 783-793

  • DOI: https://doi.org/10.1016/s0022-2836(03)00887-8
  • Primary Citation of Related Structures:  
    1NH2, 1NVP

  • PubMed Abstract: 

    RNA polymerase II-dependent transcription requires the assembly of a multi-protein, preinitiation complex on core promoter elements. Transcription factor IID (TFIID) comprising the TATA box-binding protein (TBP) and TBP-associated factors (TAFs) is responsible for promoter recognition in this complex. Subsequent association of TFIIA and TFIIB provides enhanced complex stability. TFIIA is required for transcriptional stimulation by certain viral and cellular activators, and favors formation of the preinitiation complex in the presence of repressor NC2. The X-ray structures of human and yeast TBP/TFIIA/DNA complexes at 2.1A and 1.9A resolution, respectively, are presented here and seen to resemble each other closely. The interactions made by human TFIIA with TBP and DNA within and upstream of the TATA box, including those involving water molecules, are described and compared to the yeast structure. Of particular interest is a previously unobserved region of TFIIA that extends the binding interface with TBP in the yeast, but not in the human complex, and that further elucidates biochemical and genetic results.


  • Organizational Affiliation

    ETH Zürich, Institute for Molecular Biology and Biophysics, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
TATA box binding proteinC [auth A]181Homo sapiensMutation(s): 0 
Gene Names: TBP OR TFIID OR TF2D
UniProt & NIH Common Fund Data Resources
Find proteins for P20226 (Homo sapiens)
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Go to UniProtKB:  P20226
PHAROS:  P20226
GTEx:  ENSG00000112592 
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UniProt GroupP20226
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription initiation factor IIA alpha chainD [auth B]57Homo sapiensMutation(s): 0 
Gene Names: GTF2A1 OR TF2A1
UniProt & NIH Common Fund Data Resources
Find proteins for P52655 (Homo sapiens)
Explore P52655 
Go to UniProtKB:  P52655
PHAROS:  P52655
GTEx:  ENSG00000165417 
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UniProt GroupP52655
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription initiation factor IIA beta chainE [auth C]76Homo sapiensMutation(s): 0 
Gene Names: GTF2A1 OR TF2A1
UniProt & NIH Common Fund Data Resources
Find proteins for P52655 (Homo sapiens)
Explore P52655 
Go to UniProtKB:  P52655
PHAROS:  P52655
GTEx:  ENSG00000165417 
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Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP52655
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription initiation factor IIA gamma chainF [auth D]108Homo sapiensMutation(s): 0 
Gene Names: GTF2A2 OR TF2A2
UniProt & NIH Common Fund Data Resources
Find proteins for P52657 (Homo sapiens)
Explore P52657 
Go to UniProtKB:  P52657
PHAROS:  P52657
GTEx:  ENSG00000140307 
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UniProt GroupP52657
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-D(*GP*GP*GP*GP*GP*GP*GP*CP*TP*AP*TP*AP*AP*AP*AP*GP*G)-3'A [auth E]17N/A
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*CP*CP*TP*TP*TP*TP*AP*TP*AP*GP*CP*CP*CP*CP*CP*CP*C)-3'B [auth F]17N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.229 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.624α = 90
b = 90.884β = 90
c = 125.256γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-10-21
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references