2KYV

Hybrid solution and solid-state NMR structure ensemble of phospholamban pentamer

2KYV の概要

• エントリーDOI: 10.2210/pdb2kyv/pdb
• 関連するPDBエントリー: 2KB7 2M3B
• 分子名称: Phospholamban (1 entity in total)
• 機能のキーワード: phospholamban, membrane protein, solid state nmr, hybrid method
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 30497.49

構造登録者

Verardi, R.,Shi, L.,Traaseth, N.J.,Veglia, G. (登録日: 2010-06-08, 公開日: 2011-05-11, 最終更新日: 2024-05-01)

主引用文献

Verardi, R.,Shi, L.,Traaseth, N.J.,Walsh, N.,Veglia, G.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Proc.Natl.Acad.Sci.USA, 108:9101-9106, 2011

PubMed Abstract: Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and solid-state NMR method. In lipid bilayers, PLN adopts a pinwheel topology with a narrow hydrophobic pore, which excludes ion transport. In the T state, the cytoplasmic amphipathic helices (domains Ia) are absorbed into the lipid bilayer with the transmembrane domains arranged in a left-handed coiled-coil configuration, crossing the bilayer with a tilt angle of approximately 11° with respect to the membrane normal. The tilt angle difference between the monomer and pentamer is approximately 13°, showing that intramembrane helix-helix association forces dominate over the hydrophobic mismatch, driving the overall topology of the transmembrane assembly. Our data reveal that both topology and function of PLN are shaped by the interactions with lipids, which fine-tune the regulation of SERCA.

PubMed: 21576492
DOI: 10.1073/pnas.1016535108

実験手法

SOLID-STATE NMR
SOLUTION NMR