1IUK

The structure of native ID.343 from Thermus thermophilus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.234 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of a conserved CoA-binding protein synthesized by a cell-free system.

Wada, T.Shirouzu, M.Terada, T.Ishizuka, Y.Matsuda, T.Kigawa, T.Kuramitsu, S.Park, S.Y.Tame, J.R.Yokoyama, S.

(2003) Acta Crystallogr D Biol Crystallogr 59: 1213-1218

  • DOI: https://doi.org/10.1107/s0907444903010515
  • Primary Citation of Related Structures:  
    1IUK, 1IUL

  • PubMed Abstract: 

    TT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466.


  • Organizational Affiliation

    RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
hypothetical protein TT1466140Thermus thermophilusMutation(s): 0 
UniProt
Find proteins for Q8GHJ5 (Thermus thermophilus)
Explore Q8GHJ5 
Go to UniProtKB:  Q8GHJ5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8GHJ5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.234 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 27.908α = 90
b = 64.581β = 90
c = 67.858γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
MOLREPphasing
X-PLORrefinement
HKL-2000data reduction

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2003-07-15
    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: 2014-04-16
    Changes: Other
  • Version 1.4: 2023-10-25
    Changes: Data collection, Database references, Refinement description