6MYK

Pleurotus ostreatus OstreolysinA mutant E69A with Bis-Tris

6MYK の概要

• エントリーDOI: 10.2210/pdb6myk/pdb
• 分子名称: Ostreolysin A6, 1,2-ETHANEDIOL, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: beta-sandwich fold, membrane binding protein, membrane protein
• 由来する生物種: Pleurotus ostreatus (Oyster mushroom)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61264.44

構造登録者

Tomchick, D.R.,Radhakrishnan, A.,Endapally, S. (登録日: 2018-11-01, 公開日: 2019-02-13, 最終更新日: 2023-10-11)

主引用文献

Endapally, S.,Frias, D.,Grzemska, M.,Gay, A.,Tomchick, D.R.,Radhakrishnan, A.
Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes.
Cell, 176:1040-, 2019

PubMed Abstract: Sphingomyelin and cholesterol are essential lipids that are enriched in plasma membranes of animal cells, where they interact to regulate membrane properties and many intracellular signaling processes. Despite intense study, the interaction between these lipids in membranes is not well understood. Here, structural and biochemical analyses of ostreolysin A (OlyA), a protein that binds to membranes only when they contain both sphingomyelin and cholesterol, reveal that sphingomyelin adopts two distinct conformations in membranes when cholesterol is present. One conformation, bound by OlyA, is induced by stoichiometric, exothermic interactions with cholesterol, properties that are consistent with sphingomyelin/cholesterol complexes. In its second conformation, sphingomyelin is free from cholesterol and does not bind OlyA. A point mutation abolishes OlyA's ability to discriminate between these two conformations. In cells, levels of sphingomyelin/cholesterol complexes are held constant over a wide range of plasma membrane cholesterol concentrations, enabling precise regulation of the chemical activity of cholesterol.

PubMed: 30712872
DOI: 10.1016/j.cell.2018.12.042

実験手法

X-RAY DIFFRACTION (1.8 Å)