Structure of thioredoxin from Trypanosoma brucei brucei

Sammanfattning

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

Nyckelord

Thioredoxin; Redox active disulfide; X-ray structure; Trypanosoma brucei brucei

Publicerad i

FEBS Letters
2003, volym: 554, nummer: 3, sidor: 301-305
Utgivare: ELSEVIER SCIENCE BV

SLU författare

• Eklund, Hans

  • Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
    

• Friemann, Rosmarie

  • Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Molekylärbiologi

Publikationens identifierare

• DOI: https://doi.org/10.1016/S0014-5793(03)01173-6

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/822