4WIT

TMEM16 lipid scramblase in crystal form 2

4WIT の概要

• エントリーDOI: 10.2210/pdb4wit/pdb
• 関連するPDBエントリー: 4WIS
• 分子名称: Predicted protein, CALCIUM ION (2 entities in total)
• 機能のキーワード: membrane protein, calcium activation, transport protein, lipid transport
• 由来する生物種: Nectria haematococca
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 166560.33

構造登録者

Dutzler, R.,Brunner, J.D.,Lim, N.K.,Schenck, S. (登録日: 2014-09-26, 公開日: 2014-11-12, 最終更新日: 2024-05-08)

主引用文献

Brunner, J.D.,Lim, N.K.,Schenck, S.,Duerst, A.,Dutzler, R.
X-ray structure of a calcium-activated TMEM16 lipid scramblase.
Nature, 516:207-212, 2014

PubMed Abstract: The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca(2+)-activated chloride channels as well as lipid scramblases and cation channels. Here we present the crystal structure of a TMEM16 family member from the fungus Nectria haematococca that operates as a Ca(2+)-activated lipid scramblase. Each subunit of the homodimeric protein contains ten transmembrane helices and a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca(2+)-binding site located within the hydrophobic core of the membrane. Mutations of residues involved in Ca(2+) coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl(-) channel TMEM16A. The structure reveals the general architecture of the family and its mode of Ca(2+) activation. It also provides insight into potential scrambling mechanisms and serves as a framework to unravel the conduction of ions in certain TMEM16 proteins.

PubMed: 25383531
DOI: 10.1038/nature13984

実験手法

X-RAY DIFFRACTION (3.4 Å)