Structure of thioredoxin from Trypanosoma brucei brucei

FEBS Letters

Krauth-Siegel, R.Luise³  Schmidt, Heide³  Eklund, Hans²  Forstner, Michael²  Ramaswamy, S.¹  Friemann, Rosmarie² 

[1] Department of Biochemistry, The University of Iowa, Iowa City, IA 52242, USA;Department of Molecular Biosciences, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-75124 Uppsala, Sweden;Biochemie-Zentrum Heidelberg, Universität Heidelberg, D-69120 Heidelberg, Germany

关键词: Thioredoxin;    Redox active disulfide;    X-ray structure;    Trypanosoma brucei brucei;   

DOI  :  10.1016/S0014-5793(03)01173-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown