| First Author | Lyon AM | Year | 2013 |
| Journal | Nat Struct Mol Biol | Volume | 20 |
| Issue | 3 | Pages | 355-62 |
| PubMed ID | 23377541 | Mgi Jnum | J:245284 |
| Mgi Id | MGI:5915907 | Doi | 10.1038/nsmb.2497 |
| Citation | Lyon AM, et al. (2013) Full-length Galpha(q)-phospholipase C-beta3 structure reveals interfaces of the C-terminal coiled-coil domain. Nat Struct Mol Biol 20(3):355-62 |
| abstractText | Phospholipase C-beta (PLCbeta) is directly activated by Galphaq, 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 PLCbeta3 in complex with mouse Galphaq. 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 Galphaq 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. |
