2026-02-18 REL RCSB INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY RCSB RCSB 2025-09-16 2026-02-18 2026-02-18 2026-02-18 National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) 1F32 GM145110 United States National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) 1R01 HL141076 United States National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) 1R01 GM152701 United States Gbg crosslinked to PLCb3 - second conformation Fisher IJ Lyon AM G protein, heterotrimeric G protein, lipase, phospholipase, SIGNALING PROTEIN Fisher IJ Senarath K Outlaw K Muralidharan K Garland-Kuntz EE Van Camp M Komay T Inoue A Kostenis E Lambert NA Lyon AM G beta gamma engages PLC beta 3 at multiple sites to reorient and facilitate its activation. Biorxiv US 2026 41648476 doi:10.64898/2026.01.14.699417 2692-8205 9yap FULLOVERLAP PDB 9Y7H unspecified PDB 9YAO unspecified EMDB EMD-72733 associated EM volume
Gbg crosslinked to PLCb3 - second conformation
 BMPEG-crosslinked complex of Gb1g2 and PLCb3 BMPEG-crosslinked complex of Gb1g2 and PLCb3 0 1 2 3 Homo sapiens 0.156 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Homo sapiens 0.099653891 1 Spodoptera frugiperda LEVO MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMCVDTLDISSIRDTRTGRYAR LPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTK LKLQVNQDGRIPVKNILKMFSADKKRVETALESSGLKFNRSESIRPDEFSLEIFERFLNKLSLRPDIDKILLEIGAKGKP YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEENGILPLEALDLSTDM TQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGSRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAET AFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPD SAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEGLNRGPYVLGPADREDEE EDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEY NKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVI VDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAF EEGGKFVGHRILPVSAIRSGYHYVSLRNEANQPLSLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAAL IGE Q01970 3.1.4.11 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 Bos taurus 0.037285733999999994 1 Trichoplusia ni LEVO SELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLII WDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSS GDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAF ATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVT DDGMAVATGSWDSFLKIWN P62871 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 Bos taurus 0.007861143 1 Trichoplusia ni LEVO MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFREKKFFCAIL P63212 singleParticle particle 1 7.4
20 mM HEPES pH 7.4, 100 mM NaCl, 0.1 mM EDTA and 0.1 mM EGTA
 ETHANE FEI VITROBOT MARK IV TFS KRIOS FLOOD BEAM BRIGHT FIELD FIELD EMISSION GUN 300 1.0 3.0 GATAN K3 BIOQUANTUM (6k x 4k) 53.69 1 CTFFIND PHASE FLIPPING AND AMPLITUDE CORRECTION 4GNK
PDB ID 4GNK was used as the initial model of PLCb3, and PDB ID 1GP2 as the initial model of Gbg.
 4.5 FSC 0.143 CUT-OFF Coot PHENIX 142175 MAXIMUM LIKELIHOOD MAXIMUM LIKELIHOOD cryoSPARC emd_72733.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 640 640 640 0 0 0 640 640 640 344.96 344.96 344.96 90.0 90.0 90.0 X Y Z -0.11034197 0.21638866 0.00015941744 0.0037979765 0.539 0.539 0.539 0.03 AUTHOR 4GNK PDB experimental model 1GP2 PDB experimental model FLEXIBLE FIT
Crystal structures of Gbetagamma and PLCbeta3 (PDB IDs 1GP2 and 4GNK) were rigid-body fit into the cryo-EM map using Chimera. The model was refined using molecular dynamic flexible fitting (MDFF). MDFF configuration files were generated using VMD. During MDFF simulation, Gbetagamma was set as rigid with domain restraints. The MDFF simulation was conducted with a grid scaling value of 0.5 for 100 ps, followed by 3,000 steps of energy minimization until convergence of the protein RMSD. The MDFF generated model was inspected and manually adjusted in Coot, guided through the use of deep-learning-based amino-acid-wise model quality (DAQ) scoring, and refined in PHENIX.
 emd_72733_half_map_2.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 640 640 640 0 0 0 640 640 640 344.96 344.96 344.96 90.0 90.0 90.0 X Y Z -0.0532098 0.120611936 0.00015911764 0.006380387 0.539 0.539 0.539 AUTHOR emd_72733_half_map_1.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 640 640 640 0 0 0 640 640 640 344.96 344.96 344.96 90.0 90.0 90.0 X Y Z -0.053601075 0.117454395 0.00016010704 0.0064301263 0.539 0.539 0.539 AUTHOR