Open AccessNMR Solution Structure of an Oxidised Thioredoxin h from the Eukaryotic Green Alga Chlamydomonas reinhardtii
Author(s) -
Mittard Virginie,
Blackledge Martin J.,
Stein Mariana,
Jacquot JeanPierre,
Marion Dominique,
Lancelin JeanMarc
Publication year - 1997
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1997.0374a.x
Subject(s) - thioredoxin , chlamydomonas reinhardtii , ferredoxin thioredoxin reductase , dihedral angle , substrate (aquarium) , biochemistry , biology , chemistry , crystallography , hydrogen bond , thioredoxin reductase , enzyme , molecule , gene , organic chemistry , ecology , mutant
NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydomonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 φ dihedral restraints. The structure of C. reinhardtii thioredoxin h was solved in its oxidised form, and the ensemble of 23 converged structures superpose to the geometric average structure with an atomic rmsd of 0.080 nm ± 0.016 for the (N, Cα, C) backbone atoms of residues 4–110. Comparisons with other thioredoxins, such as thioredoxin from the bacterium Escherichia coli , thioredoxin 2 from a cyanobacterium of the Anahaena genus, and human thioredoxin, showed that thioredoxin h models share more structural features with human thioredoxin than with other bacterial thioredoxins. Examination of the accessible surface around the redox‐active peptide sequence indicates that a potent thioredoxin‐ h –substrate interaction could be similar to the vertebrate thioredoxin–substrate interactions.