In:
European Journal of Biochemistry, Wiley, Vol. 243, No. 1-2 ( 1997-01), p. 374-383
Kurzfassung:
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.
Materialart:
Online-Ressource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1997.243.issue-1-2
DOI:
10.1111/j.1432-1033.1997.0374a.x
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
1997
ZDB Id:
1398347-7
ZDB Id:
2172518-4
SSG:
12
