3G3U

Crystal structure of a eukaryotic polyphosphate polymerase in complex with pyrophosphate

3G3U の概要

• エントリーDOI: 10.2210/pdb3g3u/pdb
• 関連するPDBエントリー: 3g3o 3g3q 3g3r 3g3t
• 分子名称: Vacuolar transporter chaperone 4, PYROPHOSPHATE 2-, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: polyphosphate polymerase, polyphosphate kinase, vtc complex, vacuolar transporter chaperone, tunnel enzyme, membrane, phosphoprotein, transmembrane, vacuole, biosynthetic protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Vacuole membrane; Multi-pass membrane protein: P47075
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70905.96

構造登録者

Hothorn, M. (登録日: 2009-02-02, 公開日: 2009-05-05, 最終更新日: 2023-09-06)

主引用文献

Hothorn, M.,Neumann, H.,Lenherr, E.D.,Wehner, M.,Rybin, V.,Hassa, P.O.,Uttenweiler, A.,Reinhardt, M.,Schmidt, A.,Seiler, J.,Ladurner, A.G.,Herrmann, C.,Scheffzek, K.,Mayer, A.
Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase.
Science, 324:513-516, 2009

PubMed Abstract: Polyphosphate (polyP) occurs ubiquitously in cells, but its functions are poorly understood and its synthesis has only been characterized in bacteria. Using x-ray crystallography, we identified a eukaryotic polyphosphate polymerase within the membrane-integral vacuolar transporter chaperone (VTC) complex. A 2.6 angstrom crystal structure of the catalytic domain grown in the presence of adenosine triphosphate (ATP) reveals polyP winding through a tunnel-shaped pocket. Nucleotide- and phosphate-bound structures suggest that the enzyme functions by metal-assisted cleavage of the ATP gamma-phosphate, which is then in-line transferred to an acceptor phosphate to form polyP chains. Mutational analysis of the transmembrane domain indicates that VTC may integrate cytoplasmic polymer synthesis with polyP membrane translocation. Identification of the polyP-synthesizing enzyme opens the way to determine the functions of polyP in lower eukaryotes.

PubMed: 19390046
DOI: 10.1126/science.1168120

実験手法

X-RAY DIFFRACTION (2.07 Å)