1T00

The structure of thioredoxin from S. coelicolor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.51 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.176 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor.

Stefankova, P.Maderova, J.Barak, I.Kollarova, M.Otwinowski, Z.

(2005) Acta Crystallogr Sect F Struct Biol Cryst Commun 61: 164-168

  • DOI: https://doi.org/10.1107/S1744309104032993
  • Primary Citation of Related Structures:  
    1T00

  • PubMed Abstract: 

    Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. In turn, they are reduced by electrons obtained from the NADPH-containing thioredoxin reductase. Thioredoxins have been isolated and characterized from a large number of organisms. The Gram-positive bacterium Streptomyces coelicolor contains three thioredoxins that are involved in unknown biological processes. trxA from S. coelicolor was cloned and expressed in Escherichia coli and the protein purified and crystallized using the hanging-drop method of vapour diffusion. The crystal structure of thioredoxin A has been determined at 1.5 A resolution using a synchrotron-radiation source. The protein reveals a thioredoxin-like fold with a typical CXXC active site. The crystal exhibits the symmetry of space group P2(1)2(1)2, with unit-cell parameters a = 43.6, b = 71.8, c = 33.2 A.


  • Organizational Affiliation

    Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynska dolina CH-1, 842 15 Bratislava, Slovak Republic.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thioredoxin112Streptomyces coelicolor A3(2)Mutation(s): 0 
Gene Names: TRXASCO3889SCH24.11C
UniProt
Find proteins for P52230 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
Explore P52230 
Go to UniProtKB:  P52230
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP52230
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.51 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.174 
  • R-Value Observed: 0.176 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.579α = 90
b = 71.756β = 90
c = 33.187γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-01-25
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references