4QJ3

Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with Galphaq

4QJ3 の概要

• エントリーDOI: 10.2210/pdb4qj3/pdb
• 関連するPDBエントリー: 4QJ4 4QJ5
• 分子名称: Guanine nucleotide-binding protein G(q) subunit alpha, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: gtp-binding protein alpha subunits, phospholipase c beta, ph domain, ef hand, c2 domain, tim barrel domain, gtp hydrolysis, g-protein signaling, lipase, calcium binding, gtp binding, phospholipids, membrane, signaling protein-hydrolase complex, signaling protein/hydrolase
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus : P21279; Membrane; Peripheral membrane protein: Q01970
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 135616.30

構造登録者

Lyon, A.M.,Tesmer, J.J.G. (登録日: 2014-06-03, 公開日: 2014-10-22, 最終更新日: 2023-09-20)

主引用文献

Lyon, A.M.,Begley, J.A.,Manett, T.D.,Tesmer, J.J.
Molecular mechanisms of phospholipase C beta 3 autoinhibition.
Structure, 22:1844-1854, 2014

PubMed Abstract: Phospholipase C β (PLCβ) enzymes are dramatically activated by heterotrimeric G proteins. Central to this response is the robust autoinhibition of PLCβ by the X-Y linker region within its catalytic core and by the Hα2' helix in the C-terminal extension of the enzyme. The molecular mechanism of each and their mutual dependence are poorly understood. Herein, it is shown that distinct regions within the X-Y linker have specific roles in regulating activity. Most important,an acidic stretch within the linker stabilizes a lid that occludes the active site, consistent with crystal structures of variants lacking this region. Inhibition by the Hα2' helix is independent of the X-Y linker and likely regulates activity by limiting membrane interaction of the catalytic core. Full activation of PLCβ thus requires multiple independent molecular events induced by membrane association of the catalytic core and by the binding of regulatory proteins.

PubMed: 25435326
DOI: 10.1016/j.str.2014.10.008

実験手法

X-RAY DIFFRACTION (3 Å)