Structure of thioredoxin from Trypanosoma brucei brucei.
The three-dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4 A resolution. The overall structure is more similar to that of human thioredoxin than to any other thioredoxin structure. The most striking difference to other thioredoxins is the absence of a buried carboxylate behind the active site cysteines. Instead of the common Asp, there is a Trp that binds an ordered water molecule probably involved in the protonation/deprotonation of the more buried cysteine during catalysis. The conserved Trp in the WCGPC sequence motif has an exposed position that can interact with target proteins.
Friemann
Rosmarie
R
Department of Molecular Biosciences, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-75124 Uppsala, Sweden.
Schmidt
Heide
H
Ramaswamy
S
S
Forstner
Michael
M
Krauth-Siegel
R Luise
RL
Eklund
Hans
H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013879:Thioredoxins / Q000737:chemistry* / Q000235:genetics; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000235:genetics; D014364:Tryptophan / Q000235:genetics
D011994:Recombinant Proteins; D013879:Thioredoxins; D014364:Tryptophan