Structure of thioredoxin from Trypanosoma brucei brucei

被引：23

作者：

Friemann, R

Schmidt, H

Ramaswamy, S

Forstner, M

Krauth-Siegel, RL

Eklund, H

机构：

[1] Swedish Univ Agr Sci, Dept Mol Biosci, S-75124 Uppsala, Sweden

[2] Heidelberg Univ, Biochem Zentrum Heidelberg, D-69120 Heidelberg, Germany

[3] Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA

来源：

FEBS LETTERS | 2003年 / 554卷 / 03期

关键词：

thioredoxin; redox active disulfide; X-ray structure; Trypanosoma brucei brucei;

D O I：

10.1016/S0014-5793(03)01173-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：301 / 305

页数：5

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