8GHG

Cryo-EM structure of hSlo1 in digitonin, Ca2+-free and EDTA-free

8GHG の概要

• エントリーDOI: 10.2210/pdb8ghg/pdb
• EMDBエントリー: 40038 40044 40045
• 分子名称: Calcium-activated potassium channel subunit alpha-1 (1 entity in total)
• 機能のキーワード: slo1, bk channel, ca2+- and voltage-activated k+ channel, ion channel, transport protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 483632.50

構造登録者

Tao, X.,Zhao, C.,MacKinnon, R. (登録日: 2023-03-10, 公開日: 2023-05-10, 最終更新日: 2025-06-04)

主引用文献

Tao, X.,Zhao, C.,MacKinnon, R.
Membrane protein isolation and structure determination in cell-derived membrane vesicles.
Proc.Natl.Acad.Sci.USA, 120:e2302325120-e2302325120, 2023

PubMed Abstract: Integral membrane protein structure determination traditionally requires extraction from cell membranes using detergents or polymers. Here, we describe the isolation and structure determination of proteins in membrane vesicles derived directly from cells. Structures of the ion channel Slo1 from total cell membranes and from cell plasma membranes were determined at 3.8 Å and 2.7 Å resolution, respectively. The plasma membrane environment stabilizes Slo1, revealing an alteration of global helical packing, polar lipid, and cholesterol interactions that stabilize previously unresolved regions of the channel and an additional ion binding site in the Ca regulatory domain. The two methods presented enable structural analysis of both internal and plasma membrane proteins without disrupting weakly interacting proteins, lipids, and cofactors that are essential to biological function.

PubMed: 37098056
DOI: 10.1073/pnas.2302325120

実験手法

ELECTRON MICROSCOPY (3.3 Å)