biostudies-literatureUnknown17(1)Luo MfundingGuanine nucleotide-binding (G) proteins, namely, phosphate-binding (P) loop GTPases, play a critical role in life processes among different species. Based on the structural characteristics, G proteins can be divided into heterotrimeric G proteins, small G proteins and multiple unique unconventional G proteins. The highly conserved unconventional G protein YchF is composed of a core G domain, an inserted coiled-coil domain, and a TGS domain from the N-terminus to the C-terminus. In this review, we compared the structural characteristics of the G domain in rice OsYchF1 with those of <i>Rattus norvegicus</i> heterotrimeric G protein α-subunit and human small G protein Ras-related G protein C and analyzed the binding modes of these G proteins with GTP or ATP by performing molecular dynamics siPlant signaling & behavior2024405https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959515biostudies-literatureStructural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.PMC8959515Liu YLiu LLuo MHuang GMiao RLu JHan ZLi RfalseStructural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.Guanine nucleotide-binding (G) proteins, namely, phosphate-binding (P) loop GTPases, play a critical role in life processes among different species. Based on the structural characteristics, G proteins can be divided into heterotrimeric G proteins, small G proteins and multiple unique unconventional G proteins. The highly conserved unconventional G protein YchF is composed of a core G domain, an inserted coiled-coil domain, and a TGS domain from the N-terminus to the C-terminus. In this review, we compared the structural characteristics of the G domain in rice OsYchF1 with those of <i>Rattus norvegicus</i> heterotrimeric G protein α-subunit and human small G protein Ras-related G protein C and analyzed the binding modes of these G proteins with GTP or ATP by performing molecular dynamics si2022-01-01T00:00:00Z2022 Dec2025-04-05T00:39:56.011Z2024-11-13T22:34:17.73ZS-EPMC89595153513541410.1080/15592324.2021.2024405