7SQ2

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

Replaces:  3OHM

Summary for 7SQ2

• Entry DOI: 10.2210/pdb7sq2/pdb
• Descriptor: Guanine nucleotide-binding protein G(q) subunit alpha, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, TETRAFLUOROALUMINATE ION, ... (8 entities in total)
• Functional Keywords: g-protein signaling phopholipase-c hydrolase guanine nucleotide-binding protein g(q) alpha, signaling protein
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 2
• Total formula weight: 139169.89

Authors

Endo-Streeter, S.T.,Sondek, J.,Harden, T.K. (deposition date: 2021-11-04, release date: 2021-11-17, Last modification date: 2023-10-18)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)