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TitleFull-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 3, Page 355-362, Year 2013
Publish dateFeb 3, 2013
AuthorsAngeline M Lyon / Somnath Dutta / Cassandra A Boguth / Georgios Skiniotis / John J G Tesmer /
PubMed AbstractPhospholipase 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 ...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.
External linksNat Struct Mol Biol / PubMed:23377541 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution4 - 21.0 Å
Structure data

EMDB-2271:
Cryo EM map of the Gaalphaq-PLCbeta3 complex.
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-5561:
Cryo EM map of the Gaalphaq-PLCbeta3 complex.
Method: EM (single particle) / Resolution: 19.0 Å

PDB-4gnk:
Crystal structure of Galphaq in complex with full-length human PLCbeta3
Method: X-RAY DIFFRACTION / Resolution: 4 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsGTP-BINDING PROTEIN/HYDROLASE / 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

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