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Structure of thioredoxin from Trypanosoma brucei brucei
Rosmarie Friemann1, Heide Schmidt, S Ramaswamy
1Department of Molecular Biosciences, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-75124 Uppsala, Sweden.
Abstract:
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.