5NYM

Crystal structure of the atypical poplar thioredoxin-like2.1 in reduced state


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.

Chibani, K.Saul, F.Didierjean, C.Rouhier, N.Haouz, A.

(2018) FEBS Lett 592: 1030-1041

  • DOI: https://doi.org/10.1002/1873-3468.13009
  • Primary Citation of Related Structures:  
    5NYK, 5NYL, 5NYM, 5NYN, 5NYO

  • PubMed Abstract: 

    Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.


  • Organizational Affiliation

    UMR 1136, Interactions Arbres-Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandœuvre-lès-Nancy, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thioredoxin-like protein 2.1122Populus tremula x Populus tremuloidesMutation(s): 0 
UniProt
Find proteins for I0BZV0 (Populus tremula x Populus tremuloides)
Explore I0BZV0 
Go to UniProtKB:  I0BZV0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupI0BZV0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.546α = 90
b = 52.946β = 90
c = 59.145γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
INRA-FORMAS programFrance--
Institut PasteurFrance--

Revision History  (Full details and data files)

  • Version 1.0: 2018-02-28
    Type: Initial release
  • Version 1.1: 2018-04-04
    Changes: Data collection, Database references