1DBY

NMR STRUCTURES OF CHLOROPLAST THIOREDOXIN M CH2 FROM THE GREEN ALGA CHLAMYDOMONAS REINHARDTII


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 28 
  • Selection Criteria: STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY. STRUCTURES WITH FAVORABLE NON- BOND ENERGY. STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS. STRUCTURES WITH THE LOWEST ENERGY. 

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This is version 1.3 of the entry. See complete history


Literature

NMR structures of thioredoxin m from the green alga Chlamydomonas reinhardtii.

Lancelin, J.M.Guilhaudis, L.Krimm, I.Blackledge, M.J.Marion, D.Jacquot, J.P.

(2000) Proteins 41: 334-349

  • DOI: https://doi.org/10.1002/1097-0134(20001115)41:3<334::aid-prot60>3.3.co;2-d
  • Primary Citation of Related Structures:  
    1DBY

  • PubMed Abstract: 

    Chloroplast thioredoxin m from the green alga Chlamydomomas reinhardtii is very efficiently reduced in vitro and in vivo in the presence of photoreduced ferredoxin and a ferredoxin dependent ferredoxin-thioredoxin reductase. Once reduced, thioredoxin m has the capability to quickly activate the NADP malate dehydrogenase (EC 1.1.1.82) a regulatory enzyme involved in an energy-dependent assimilation of carbon dioxide in C4 plants. This activation is the result of the reduction of two disulfide bridges by thioredoxin m, that are located at the N- and C-terminii of the NADP malate dehydrogenase. The molecular structure of thioredoxin m was solved using NMR and compared to other known thioredoxins. Thioredoxin m belongs to the prokaryotic type of thioredoxin, which is divergent from the eukaryotic-type thioredoxins also represented in plants by the h (cytosolic) and f (chloroplastic) types of thioredoxins. The dynamics of the molecule have been assessed using (15)N relaxation data and are found to correlate well with regions of disorder found in the calculated NMR ensemble. The results obtained provide a novel basis to interpret the thioredoxin dependence of the activation of chloroplast NADP-malate dehydrogenase. The specific catalytic mechanism that takes place in the active site of thioredoxins is also discussed on the basis of the recent new understanding and especially in the light of the dual general acid-base catalysis exerted on the two cysteines of the redox active site. It is proposed that the two cysteines of the redox active site may insulate each other from solvent attack by specific packing of invariable hydrophobic amino acids.


  • Organizational Affiliation

    Laboratoire de RMN Biomoléculaire associé au CNRS, Université Claude Bernard-Lyon 1 and Ecole Supérieure de Chimie, Physique et Electronique de Lyon, Villeurbanne, France. lancelin@hikari.cpe.fr


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHLOROPLAST THIOREDOXIN M CH2107Chlamydomonas reinhardtiiMutation(s): 0 
Gene Names: NUCLEAR
UniProt
Find proteins for P23400 (Chlamydomonas reinhardtii)
Explore P23400 
Go to UniProtKB:  P23400
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23400
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 28 
  • Selection Criteria: STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY. STRUCTURES WITH FAVORABLE NON- BOND ENERGY. STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS. STRUCTURES WITH THE LOWEST ENERGY. 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-11-08
    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: 2022-02-16
    Changes: Data collection, Database references, Derived calculations