8VGA

Crystal Structure of Guanine Nucleotide-Binding Protein (G Protein) Alpha-1 Subunit from Selaginella moellendorffii in complex with GTP gamma S

8VGA の概要

• エントリーDOI: 10.2210/pdb8vga/pdb
• 関連するPDBエントリー: 8VGB
• 分子名称: Guanine nucleotide-binding protein alpha subunit, MAGNESIUM ION, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: g protein, alpha subunit, smgpa1, elaginella moellendorffii, signaling protein
• 由来する生物種: Selaginella moellendorffii (Spikemoss)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87677.54

構造登録者

Lee, S.G.,Jez, J.M. (登録日: 2023-12-27, 公開日: 2024-11-06)

主引用文献

Torres-Rodriguez, M.D.,Lee, S.G.,Roy Choudhury, S.,Paul, R.,Selvam, B.,Shukla, D.,Jez, J.M.,Pandey, S.
Structure-function analysis of plant G-protein regulatory mechanisms identifies key G alpha-RGS protein interactions.
J.Biol.Chem., 300:107252-107252, 2024

PubMed Abstract: Heterotrimeric GTP-binding protein alpha subunit (Gα) and its cognate regulator of G-protein signaling (RGS) protein transduce signals in eukaryotes spanning protists, amoeba, animals, fungi, and plants. The core catalytic mechanisms of the GTPase activity of Gα and the interaction interface with RGS for the acceleration of GTP hydrolysis seem to be conserved across these groups; however, the RGS gene is under low selective pressure in plants, resulting in its frequent loss. Our current understanding of the structural basis of Gα:RGS regulation in plants has been shaped by Arabidopsis Gα, (AtGPA1), which has a cognate RGS protein. To gain a comprehensive understanding of this regulation beyond Arabidopsis, we obtained the x-ray crystal structures of Oryza sativa Gα, which has no RGS, and Selaginella moellendorffi (a lycophyte) Gα that has low sequence similarity with AtGPA1 but has an RGS. We show that the three-dimensional structure, protein-protein interaction with RGS, and the dynamic features of these Gα are similar to AtGPA1 and metazoan Gα. Molecular dynamic simulation of the Gα-RGS interaction identifies the contacts established by specific residues of the switch regions of GTP-bound Gα, crucial for this interaction, but finds no significant difference due to specific amino acid substitutions. Together, our data provide valuable insights into the regulatory mechanisms of plant G-proteins but do not support the hypothesis of adaptive co-evolution of Gα:RGS proteins in plants.

PubMed: 38569936
DOI: 10.1016/j.jbc.2024.107252

実験手法

X-RAY DIFFRACTION (2.57602485808 Å)