3NAG

Crystal structure of the phosphoribosylpyrophosphate (PRPP) synthetase from Thermoplasma Volcanium in complex with ADP

3NAG の概要

• エントリーDOI: 10.2210/pdb3nag/pdb
• 関連するPDBエントリー: 1U9Y 1U9Z 3LPN 3LRT 3MBI
• 分子名称: Ribose-phosphate pyrophosphokinase, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: phosphoribosyl transferase, adp binding, transferase
• 由来する生物種: Thermoplasma volcanium GSS1
• 細胞内の位置: Cytoplasm (By similarity): Q97CA5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65470.77

構造登録者

Cherney, M.M.,Cherney, L.T.,Garen, C.R.,James, M.N.G. (登録日: 2010-06-02, 公開日: 2011-06-08, 最終更新日: 2024-02-21)

主引用文献

Cherney, M.M.,Cherney, L.T.,Garen, C.R.,James, M.N.
The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs.
J.Mol.Biol., 413:844-856, 2011

PubMed Abstract: Phosphoribosyl pyrophosphate (PRPP) synthetase catalyzes the transfer of the pyrophosphate group from ATP to ribose-5-phosphate (R5P) yielding PRPP and AMP. PRPP is an essential metabolite that plays a central role in cellular metabolism. The enzyme from a thermophilic archaeon Thermoplasma volcanium (Tv) was expressed in Escherichia coli, crystallized, and its X-ray molecular structure was determined in a complex with its substrate R5P and with substrate analogs β,γ-methylene ATP and ADP in two monoclinic crystal forms, P2(1). The β,γ-methylene ATP- and the ADP-bound binary structures were determined from crystals grown from ammonium sulfate solutions; these crystals diffracted to 1.8 Å and 1.5 Å resolutions, respectively. Crystals of the ternary complex with ADP-Mg(2+) and R5P were grown from a polyethylene glycol solution in the absence of sulfate ions, and they diffracted to 1.8 Å resolution; the unit cell is approximately double the size of the unit cell of the crystals grown in the presence of sulfate. The Tv PRPP synthetase adopts two conformations, open and closed, at different stages in the catalytic cycle. The binding of substrates, R5P and ATP, occurs with PRPP synthetase in the open conformation, whereas catalysis presumably takes place with PRPP synthetase in the closed conformation. The Tv PRPP synthetase forms a biological dimer in contrast to the tetrameric or hexameric quaternary structures of the Methanocaldococcus jannaschii and Bacillus subtilis PRPP synthetases, respectively.

PubMed: 21963988
DOI: 10.1016/j.jmb.2011.09.007

実験手法

X-RAY DIFFRACTION (1.75 Å)