1AIP

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.216 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.

Wang, Y.Jiang, Y.Meyering-Voss, M.Sprinzl, M.Sigler, P.B.

(1997) Nat Struct Biol 4: 650-656

  • DOI: https://doi.org/10.1038/nsb0897-650
  • Primary Citation of Related Structures:  
    1AIP

  • PubMed Abstract: 

    In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor. The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E. coli complex, in which the monomeric E. coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat. GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP. The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins.


  • Organizational Affiliation

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ELONGATION FACTOR TU
A, B, E, F
405Thermus thermophilusMutation(s): 0 
UniProt
Find proteins for P60338 (Thermus thermophilus)
Explore P60338 
Go to UniProtKB:  P60338
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60338
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ELONGATION FACTOR TS
C, D, G, H
196Thermus thermophilusMutation(s): 0 
UniProt
Find proteins for P43895 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore P43895 
Go to UniProtKB:  P43895
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43895
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.216 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 120.3α = 90
b = 127.5β = 90.3
c = 123.7γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-10-22
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance