3QR0

Crystal Structure of S. officinalis PLC21

Summary for 3QR0

• Entry DOI: 10.2210/pdb3qr0/pdb
• Related: 3QR1
• Descriptor: phospholipase C-beta (PLC-beta), CALCIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: ph domain, ef hand, c2 domain, tim barrel domain, hydrolase, phospholipase, calcium binding, phospholipid binding
• Biological source: Sepia officinalis (cuttlefish)
• Total number of polymer chains: 1
• Total formula weight: 93740.36

Authors

Lyon, A.M.,Northup, J.K.,Tesmer, J.J.G. (deposition date: 2011-02-16, release date: 2011-08-10, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)