3QR0

Crystal Structure of S. officinalis PLC21

3QR0 の概要

• エントリーDOI: 10.2210/pdb3qr0/pdb
• 関連するPDBエントリー: 3QR1
• 分子名称: phospholipase C-beta (PLC-beta), CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ph domain, ef hand, c2 domain, tim barrel domain, hydrolase, phospholipase, calcium binding, phospholipid binding
• 由来する生物種: Sepia officinalis (cuttlefish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 93740.36

構造登録者

Lyon, A.M.,Northup, J.K.,Tesmer, J.J.G. (登録日: 2011-02-16, 公開日: 2011-08-10, 最終更新日: 2023-09-13)

主引用文献

Lyon, A.M.,Tesmer, V.M.,Dhamsania, V.D.,Thal, D.M.,Gutierrez, J.,Chowdhury, S.,Suddala, K.C.,Northup, J.K.,Tesmer, J.J.
An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galphaq activation.
Nat.Struct.Mol.Biol., 18:999-1005, 2011

PubMed Abstract: The enzyme phospholipase C-β (PLCβ) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the Gq family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCβ (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCβ3 considerably increase basal activity and diminish stimulation by Gαq. Gαq binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCβ.

PubMed: 21822282
DOI: 10.1038/nsmb.2095

実験手法

X-RAY DIFFRACTION (2 Å)