4N08
Structure of Trypanosoma brucei brucei adenosine kinase (apo)
Summary for 4N08
| Entry DOI | 10.2210/pdb4n08/pdb |
| Related | 4N09 |
| Descriptor | Adenosine kinase (2 entities in total) |
| Functional Keywords | anion hole, adenosine kinase, transferase |
| Biological source | Trypanosoma brucei brucei |
| Total number of polymer chains | 1 |
| Total formula weight | 38228.60 |
| Authors | Timm, J.,Wilson, K.S. (deposition date: 2013-10-01, release date: 2014-01-15, Last modification date: 2024-02-28) |
| Primary citation | Timm, J.,Gonzalez-Pacanowska, D.,Wilson, K.S. Structures of adenosine kinase from Trypanosoma brucei brucei. Acta Crystallogr F Struct Biol Commun, 70:34-39, 2014 Cited by PubMed Abstract: Trypanosoma brucei is a single-cellular parasite of the genus Kinetoplastida and is the causative agent of African sleeping sickness in humans. Adenosine kinase is a key enzyme in the purine-salvage pathway, phosphorylating adenosine to AMP, and also activates cytotoxic analogues such as cordycepin and Ara-A by their phosphorylation. The structures of T. brucei brucei adenosine kinase (TbAK) in its unliganded open conformation and complexed with adenosine and ADP in the closed conformation are both reported to 2.6 Å resolution. The structures give insight into the binding mode of the substrates and the conformational change induced upon substrate binding. This information can be used to guide the improvement of cytotoxic substrate analogues as potential antitrypanosomal drugs. PubMed: 24419613DOI: 10.1107/S2053230X13033621 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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