4N5A

Crystal structure of Efr3

4N5A の概要

• エントリーDOI: 10.2210/pdb4n5a/pdb
• 関連するPDBエントリー: 4N5C
• 分子名称: Protein EFR3 (1 entity in total)
• 機能のキーワード: heat-like repeats, component of stt4 complex, ypp1, plasma membrane, protein binding
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64781.94

構造登録者

Wu, X.,Chi, R.J.,Baskin, J.M.,Lucast, L.,Burd, C.G.,De Camilli, P.,Reinisch, K.M. (登録日: 2013-10-09, 公開日: 2014-01-22, 最終更新日: 2024-10-30)

主引用文献

Wu, X.,Chi, R.J.,Baskin, J.M.,Lucast, L.,Burd, C.G.,De Camilli, P.,Reinisch, K.M.
Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex.
Dev.Cell, 28:19-29, 2014

PubMed Abstract: Plasma membrane PI4P helps determine the identity of this membrane and plays a key role in signal transduction as the precursor of PI(4,5)P2 and its metabolites. Here, we report the atomic structure of the protein scaffold that is required for the plasma membrane localization and function of Stt4/PI4KIIIα, the PI 4-kinase responsible for this PI4P pool. Both proteins of the scaffold, Efr3 and YPP1/TTC7, are composed of α-helical repeats, which are arranged into a rod in Efr3 and a superhelix in Ypp1. A conserved basic patch in Efr3, which binds acidic phospholipids, anchors the complex to the plasma membrane. Stt4/PI4KIIIα is recruited by interacting with the Ypp1 C-terminal lobe, which also binds to unstructured regions in the Efr3 C terminus. Phosphorylation of this Efr3 region counteracts Ypp1 binding, thus providing a mechanism through which Stt4/PI4KIIIα recruitment, and thus a metabolic reaction of fundamental importance in cell physiology, can be regulated.

PubMed: 24360784
DOI: 10.1016/j.devcel.2013.11.012
主引用文献が同じPDBエントリー

実験手法

X-RAY DIFFRACTION (3.204 Å)