7AS6

2.0 angstrom structure of plant Extended Synaptotagmin 1, C2A domain

7AS6 の概要

• エントリーDOI: 10.2210/pdb7as6/pdb
• 分子名称: Synaptotagmin-1, CADMIUM ION, NICKEL (II) ION, ... (6 entities in total)
• 機能のキーワード: c2 domain, beta sandwich, lipid transport, contact sites, lipid binding protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17240.09

構造登録者

Benavente, J.L.,Albert, A. (登録日: 2020-10-27, 公開日: 2021-08-18, 最終更新日: 2024-01-31)

主引用文献

Benavente, J.L.,Siliqi, D.,Infantes, L.,Lagartera, L.,Mills, A.,Gago, F.,Ruiz-Lopez, N.,Botella, M.A.,Sanchez-Barrena, M.J.,Albert, A.
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites.
Life Sci Alliance, 4:-, 2021

PubMed Abstract: Non-vesicular lipid transfer at ER and plasma membrane (PM) contact sites (CS) is crucial for the maintenance of membrane lipid homeostasis. Extended synaptotagmins (E-Syts) play a central role in this process as they act as molecular tethers of ER and PM and as lipid transfer proteins between these organelles. E-Syts are proteins constitutively anchored to the ER through an N-terminal hydrophobic segment and bind the PM via a variable number of C-terminal C2 domains. Synaptotagmins (SYTs) are the plant orthologous of E-Syts and regulate the ER-PM communication in response to abiotic stress. Combining different structural and biochemical techniques, we demonstrate that the binding of SYT1 to lipids occurs through a Ca-dependent lipid-binding site and by a site for phosphorylated forms of phosphatidylinositol, thus integrating two different molecular signals in response to stress. In addition, we show that SYT1 displays three highly flexible hinge points that provide conformational freedom to facilitate lipid extraction, protein loading, and subsequent transfer between PM and ER.

PubMed: 34408000
DOI: 10.26508/lsa.202101152

実験手法

X-RAY DIFFRACTION (2 Å)