8vga

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

spinqualitylabelsall models 8vga, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vga is a 2 chain structure with sequence from Selaginella moellendorffii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5760248Å Ligands: GSP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D8QR00_SELML Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.[RuleBase:RU368109] Publication Abstract from PubMed Heterotrimeric GTP-binding protein alpha subunit (Galpha) 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 Galpha 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 Galpha:RGS regulation in plants has been shaped by Arabidopsis Galpha, (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 Galpha, which has no RGS, and Selaginella moellendorffi (a lycophyte) Galpha 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 Galpha are similar to AtGPA1 and metazoan Galpha. Molecular dynamic simulation of the Galpha-RGS interaction identifies the contacts established by specific residues of the switch regions of GTP-bound Galpha, 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 Galpha:RGS proteins in plants. Structure-function analysis of plant G-protein regulatory mechanisms identifies key Galpha-RGS protein interactions.,Torres-Rodriguez MD, Lee SG, Roy Choudhury S, Paul R, Selvam B, Shukla D, Jez JM, Pandey S J Biol Chem. 2024 May;300(5):107252. doi: 10.1016/j.jbc.2024.107252. Epub 2024 , Apr 1. PMID:38569936 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA