1F3U

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.225 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.

Gaiser, F.Tan, S.Richmond, T.J.

(2000) J Mol Biol 302: 1119-1127

  • DOI: https://doi.org/10.1006/jmbi.2000.4110
  • Primary Citation of Related Structures:  
    1F3U

  • PubMed Abstract: 

    General transcription factor IIF (TFIIF) is required for transcription by RNA polymerase II; it consists minimally of a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74. According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation. The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.


  • Organizational Affiliation

    ETH Zürich, Institut fr Molekularbiologie und Biophysik, Zürich, Switzerland.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTION INITIATION FACTOR IIF, BETA SUBUNIT
A, C, E, G
118Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P13984 (Homo sapiens)
Explore P13984 
Go to UniProtKB:  P13984
PHAROS:  P13984
GTEx:  ENSG00000188342 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP13984
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTION INITIATION FACTOR IIF, ALPHA SUBUNIT
B, D, F, H
171Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P35269 (Homo sapiens)
Explore P35269 
Go to UniProtKB:  P35269
GTEx:  ENSG00000125651 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP35269
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.225 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.015α = 104.51
b = 72.29β = 93.32
c = 82.266γ = 104.32
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-10-11
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references