1R26
Crystal structure of thioredoxin from Trypanosoma brucei brucei
Summary for 1R26
Entry DOI | 10.2210/pdb1r26/pdb |
Descriptor | Thioredoxin (2 entities in total) |
Functional Keywords | redox-active disulfide; thioredoxin, electron transport |
Biological source | Trypanosoma |
Total number of polymer chains | 1 |
Total formula weight | 14483.93 |
Authors | Friemann, R.,Schmidt, H.,Ramaswamy, S.,Forstner, M.,Krauth-Siegel, R.L.,Eklund, H. (deposition date: 2003-09-26, release date: 2003-12-09, Last modification date: 2024-11-06) |
Primary citation | Friemann, R.,Schmidt, H.,Ramaswamy, S.,Forstner, M.,Krauth-Siegel, R.L.,Eklund, H. Structure of thioredoxin from Trypanosoma brucei brucei FEBS Lett., 554:301-305, 2003 Cited by PubMed Abstract: The three-dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4 A 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. PubMed: 14623083DOI: 10.1016/S0014-5793(03)01173-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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