7SQ2

Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex

「3OHM」から置き換えられました

7SQ2 の概要

• エントリーDOI: 10.2210/pdb7sq2/pdb
• 分子名称: Guanine nucleotide-binding protein G(q) subunit alpha, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, TETRAFLUOROALUMINATE ION, ... (8 entities in total)
• 機能のキーワード: g-protein signaling phopholipase-c hydrolase guanine nucleotide-binding protein g(q) alpha, signaling protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 139169.89

構造登録者

Endo-Streeter, S.T.,Sondek, J.,Harden, T.K. (登録日: 2021-11-04, 公開日: 2021-11-17, 最終更新日: 2023-10-18)

主引用文献

Endo-Streeter, S.T.,Sondek, J.,Harden, T.K.
Kinetic Scaffolding Mediated by a Phospholipase C-{beta} and Gq Signaling Complex
Science, 330:974-980, 2010

PubMed Abstract: Transmembrane signals initiated by a broad range of extracellular stimuli converge on nodes that regulate phospholipase C (PLC)-dependent inositol lipid hydrolysis for signal propagation. We describe how heterotrimeric guanine nucleotide-binding proteins (G proteins) activate PLC-βs and in turn are deactivated by these downstream effectors. The 2.7-angstrom structure of PLC-β3 bound to activated Gα(q) reveals a conserved module found within PLC-βs and other effectors optimized for rapid engagement of activated G proteins. The active site of PLC-β3 in the complex is occluded by an intramolecular plug that is likely removed upon G protein-dependent anchoring and orientation of the lipase at membrane surfaces. A second domain of PLC-β3 subsequently accelerates guanosine triphosphate hydrolysis by Gα(q), causing the complex to dissociate and terminate signal propagation. Mutations within this domain dramatically delay signal termination in vitro and in vivo. Consequently, this work suggests a dynamic catch-and-release mechanism used to sharpen spatiotemporal signals mediated by diverse sensory inputs.

PubMed: 20966218
DOI: 10.1126/science.1193438

実験手法

X-RAY DIFFRACTION (2.6 Å)