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Full-Length Gαq–Phospholipase C-β3 Structure Reveals Interfaces of the C-terminal Coiled-Coil Domain

Authors
Journal
Nature Structural & Molecular Biology
1545-9993
Publisher
Nature Publishing Group
Publication Date
Volume
20
Issue
3
Identifiers
DOI: 10.1038/nsmb.2497
Keywords
  • Article
Disciplines
  • Biology

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 3D reconstructions of human full-length PLCβ3 in complex with murine Gαq. The distal CTD forms an extended, monomeric helical bundle consisting of three anti-parallel segments with structural similarity to membrane-binding bin–amphiphysin–Rvs (BAR) domains. Sequence conservation of the distal CTD identifies 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 the distal CTD plays roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis.

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