1TOF

THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES

Summary for 1TOF

• Entry DOI: 10.2210/pdb1tof/pdb
• Descriptor: THIOREDOXIN H (1 entity in total)
• Functional Keywords: oxidoreductase, electron transport
• Biological source: Chlamydomonas reinhardtii
• Cellular location: Cytoplasm: P80028
• Total number of polymer chains: 1
• Total formula weight: 11727.53

Authors

Mittard, V.,Blackledge, M.J.,Stein, M.,Jacquot, J.-P.,Marion, D.,Lancelin, J.-M. (deposition date: 1996-05-30, release date: 1996-12-07, Last modification date: 2024-10-30)

Primary citation

Mittard, V.,Blackledge, M.J.,Stein, M.,Jacquot, J.P.,Marion, D.,Lancelin, J.M.
NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii.
Eur.J.Biochem., 243:374-383, 1997

PubMed Abstract: NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydonmonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 phi 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, C(alpha), 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 Anabaena 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 redoxactive peptide sequence indicates that a potent thioredoxin-h-substrate interaction could be similar to the vertebrate thioredoxin-substrate interactions.

PubMed: 9030762
DOI: 10.1111/j.1432-1033.1997.0374a.x

Experimental method

SOLUTION NMR