4GNK

Crystal structure of Galphaq in complex with full-length human PLCbeta3

Summary for 4GNK

• Entry DOI: 10.2210/pdb4gnk/pdb
• Descriptor: Guanine nucleotide-binding protein G(q) subunit alpha, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, GUANOSINE-5'-DIPHOSPHATE, ... (8 entities in total)
• Functional Keywords: gtp-binding protein alpha subunits, phospholipase c beta, coiled-coil domain, ph domain, ef hand, c2 domain, tim barrel domain, phospholipase, gtp hydrolysis, g-protein signaling, membrane targeting, lipase, hydrolase, calcium binding, gtp binding, phospholipids, gtp-binding protein-hydrolase complex, gtp-binding protein/hydrolase
• Biological source: Mus musculus (mouse); More
• Cellular location: Nucleus: P21279; Membrane; Peripheral membrane protein: Q01970 Q01970
• Total number of polymer chains: 5
• Total formula weight: 393280.92

Authors

Lyon, A.M.,Tesmer, J.J.G. (deposition date: 2012-08-17, release date: 2013-02-06, Last modification date: 2023-09-13)

Primary citation

Lyon, A.M.,Dutta, S.,Boguth, C.A.,Skiniotis, G.,Tesmer, J.J.
Full-length G alpha (q)-phospholipase C-beta 3 structure reveals interfaces of the C-terminal coiled-coil domain.
Nat.Struct.Mol.Biol., 20:355-362, 2013

PubMed Abstract: Phospholipase C-β (PLCβ) is directly activated by Gαq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCβ3 in complex with mouse Gαq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments with structural similarity to membrane-binding bin-amphiphysin-Rvs (BAR) domains. Sequence conservation of the distal CTD suggests putative membrane and protein interaction sites, the latter of which bind the N-terminal helix of Gαq in both the crystal structure and cryo-EM reconstructions. Functional analysis suggests that the distal CTD has roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis.

PubMed: 23377541
DOI: 10.1038/nsmb.2497

Experimental method

X-RAY DIFFRACTION (4 Å)