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4N09

Structure of Trypanosoma brucei brucei adenosine kinase in complex with adenosine and AMPPNP

Summary for 4N09
Entry DOI10.2210/pdb4n09/pdb
Related4N08
DescriptorAdenosine kinase, ADENOSINE, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsanion hole, adenosine kinase, adenosine, amppnp, transferase
Biological sourceTrypanosoma brucei brucei
Total number of polymer chains4
Total formula weight155816.30
Authors
Timm, J.,Gonzalez-Pacanowska, D.,Wilson, K.S. (deposition date: 2013-10-01, release date: 2014-01-15, Last modification date: 2024-11-20)
Primary citationTimm, 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: 24419613
DOI: 10.1107/S2053230X13033621
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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