期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 20, 期 3, 页码 355-362出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2497
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资金
- US National Institutes of Health (NIH) [HL086865, HL071818, GM081655]
- NIH [DK090165]
- University of Michigan Biological Sciences Scholars Program
- American Heart Association
- NIH through the University of Michigan Cancer Center Support Grant [P30 CA046592]
- Michigan Economic Development Corporation and Michigan's Technology Tr-Corridor [085P100817]
- US National Cancer Institute [Y1-00-1020]
- US National Institute of General Medical Services [Y1-GM-1104]
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-06CH11357]
- [DK20572]
Phospholipase C-beta (PLC beta) is directly activated by G alpha(q), 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 PLC beta 3 in complex with mouse G alpha(q). 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 G alpha(q) 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.
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