5IIT

Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1

5IIT の概要

• エントリーDOI: 10.2210/pdb5iit/pdb
• 分子名称: Vacuolar transporter chaperone 4,Core histone macro-H2A.1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: helical bundle, alpha-helical hairpin, inositol phosphate binding protein, protein-protein interaction, chaperone
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Nucleus : O75367
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 170463.89

構造登録者

Wild, R.,Hothorn, M. (登録日: 2016-03-01, 公開日: 2016-04-27, 最終更新日: 2024-01-10)

主引用文献

Wild, R.,Gerasimaite, R.,Jung, J.Y.,Truffault, V.,Pavlovic, I.,Schmidt, A.,Saiardi, A.,Jessen, H.J.,Poirier, Y.,Hothorn, M.,Mayer, A.
Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains.
Science, 352:986-990, 2016

PubMed Abstract: Phosphorus is a macronutrient taken up by cells as inorganic phosphate (P(i)). How cells sense cellular P(i) levels is poorly characterized. Here, we report that SPX domains--which are found in eukaryotic phosphate transporters, signaling proteins, and inorganic polyphosphate polymerases--provide a basic binding surface for inositol polyphosphate signaling molecules (InsPs), the concentrations of which change in response to P(i) availability. Substitutions of critical binding surface residues impair InsP binding in vitro, inorganic polyphosphate synthesis in yeast, and P(i) transport in Arabidopsis In plants, InsPs trigger the association of SPX proteins with transcription factors to regulate P(i) starvation responses. We propose that InsPs communicate cytosolic P(i) levels to SPX domains and enable them to interact with a multitude of proteins to regulate P(i) uptake, transport, and storage in fungi, plants, and animals.

PubMed: 27080106
DOI: 10.1126/science.aad9858

実験手法

X-RAY DIFFRACTION (2.134 Å)