5C5V

Recombinant Inorganic Pyrophosphatase from T brucei brucei

5C5V の概要

• エントリーDOI: 10.2210/pdb5c5v/pdb
• 分子名称: Acidocalcisomal pyrophosphatase, IMIDODIPHOSPHORIC ACID, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: ef-hand, ppase domain, ca binding protein, hydrolase
• 由来する生物種: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80516.45

構造登録者

Jamwal, A.,Yogavel, M.,Sharma, A. (登録日: 2015-06-22, 公開日: 2015-11-04, 最終更新日: 2024-03-20)

主引用文献

Jamwal, A.,Round, A.R.,Bannwarth, L.,Venien-Bryan, C.,Belrhali, H.,Yogavel, M.,Sharma, A.
Structural and Functional Highlights of Vacuolar Soluble Protein 1 from Pathogen Trypanosoma brucei brucei
J.Biol.Chem., 290:30498-30513, 2015

PubMed Abstract: Trypanosoma 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. The 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 Mg(2+) 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 SAXS and TEM data. SAXS data suggest structural flexibility in EF hand domains indicative of conformational plasticity within TbbVSP1.

PubMed: 26494625
DOI: 10.1074/jbc.M115.674176

実験手法

X-RAY DIFFRACTION (2.35 Å)