FEBS Letters | |
Structure of thioredoxin from Trypanosoma brucei brucei | |
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
【 预 览 】
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RO201912020313536ZK.pdf | 323KB | download |