Structural highlights
FunctionPublication Abstract from PubMedTrypanosoma brucei (T. brucei) is responsible for the fatal human disease called African trypanosomiasis or sleeping sickness. The causative parasite Trypanosoma encodes soluble versions of inorganic pyrophosphatases (PPase), also called vacuolar soluble proteins (VSPs), which are localized to its acidocalcisomes. Latter are acidic membrane enclosed organelles rich in polyphosphate chains and divalent cations whose significance in these parasites remains unclear. We here report the crystal structure of T. brucei brucei acidocalcisomal PPases in a ternary complex with Mg2+ and imidodiphosphate. The crystal structure reveals a novel structural architecture distinct from known class I PPases in its tetrameric oligomeric state in which a fused EF-hand domain arranges around the catalytic PPase domain. This unprecedented assembly evident from TbbVSP1 crystal structure is further confirmed by small angle X-ray scattering (SAXS) and electron microscopy data. Solution scattering data suggests structural flexibility in EF-hand domains indicative of conformational plasticity within TbbVSP1. Structural and Functional highlights of Vacuolar Soluble Protein 1 from pathogen T. brucei. brucei.,Jamwal A, Round AR, Bannwarth L, Bryan CV, Belrahli H, Yogavel M, Sharma A J Biol Chem. 2015 Oct 22. pii: jbc.M115.674176. PMID:26494625[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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