Eklund, Hans
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
The three-dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4 Angstrom 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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved
Keywords
Thioredoxin; Redox active disulfide; X-ray structure; Trypanosoma brucei brucei
Published in
FEBS Letters
2003, volume: 554, number: 3, pages: 301-305
Publisher: ELSEVIER SCIENCE BV
SLU Authors
Friemann, Rosmarie
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
UKÄ Subject classification
Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1016/S0014-5793(03)01173-6
Permanent link to this page (URI)
https://res.slu.se/id/publ/822