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Structure of thioredoxin from Trypanosoma brucei brucei
Author(s) -
Friemann Rosmarie,
Schmidt Heide,
Ramaswamy S.,
Forstner Michael,
Krauth-Siegel R.Luise,
Eklund Hans
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01173-6
Subject(s) - trypanosoma brucei , thioredoxin , cysteine , chemistry , biochemistry , sequence motif , structural motif , biology , stereochemistry , enzyme , dna , gene
The three‐dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4 Å 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.