2M3B

Serine 16 phosphorylated phospholamban pentamer, Hybrid solution and solid-state NMR structural ensemble

2M3B の概要

• エントリーDOI: 10.2210/pdb2m3b/pdb
• 関連するPDBエントリー: 2KYV
• NMR情報: BMRB: 18952
• 分子名称: Cardiac phospholamban (1 entity in total)
• 機能のキーワード: phospholamban, pln, plb, membrane protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Sarcoplasmic reticulum membrane; Single-pass membrane protein (By similarity): P61015
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 30897.39

構造登録者

Vostrikov, V.V.,Verardi, R.,Veglia, G. (登録日: 2013-01-15, 公開日: 2013-10-30, 最終更新日: 2024-10-30)

主引用文献

Vostrikov, V.V.,Mote, K.R.,Verardi, R.,Veglia, G.
Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport.
Structure, 21:2119-2130, 2013

PubMed Abstract: Phospholamban (PLN) inhibits the sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA), thereby regulating cardiac diastole. In membranes, PLN assembles into homopentamers that in both the phosphorylated and nonphosphorylated states have been proposed to form ion-selective channels. Here, we determined the structure of the phosphorylated pentamer using a combination of solution and solid-state nuclear magnetic resonance methods. We found that the pinwheel architecture of the homopentamer is preserved upon phosphorylation, with each monomer having an L-shaped conformation. The TM domains form a hydrophobic pore approximately 24 Å long and 2 Å in diameter, which is inconsistent with canonical Ca²⁺-selective channels. Phosphorylation, however, enhances the conformational dynamics of the cytoplasmic region of PLN, causing partial unwinding of the amphipathic helix. We propose that PLN oligomers act as storage for active monomers, keeping SERCA function within a physiological window.

PubMed: 24207128
DOI: 10.1016/j.str.2013.09.008

実験手法

SOLID-STATE NMR
SOLUTION NMR