6N84

MBP-fusion protein of transducin-alpha residues 327-350

Summary for 6N84

• Entry DOI: 10.2210/pdb6n84/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose/maltodextrin-binding periplasmic protein,Guanine nucleotide-binding protein G(t) subunit alpha-2, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: g alpha, mbp, chaperone
• Biological source: Escherichia coli O157:H7; More
• Total number of polymer chains: 1
• Total formula weight: 46559.19

Authors

Srivastava, D.,Gakhar, L.,Artemyev, N.O. (deposition date: 2018-11-28, release date: 2019-07-10, Last modification date: 2024-01-10)

Primary citation

Srivastava, D.,Gakhar, L.,Artemyev, N.O.
Structural underpinnings of Ric8A function as a G-protein alpha-subunit chaperone and guanine-nucleotide exchange factor.
Nat Commun, 10:3084-3084, 2019

PubMed Abstract: Resistance to inhibitors of cholinesterase 8A (Ric8A) is an essential regulator of G protein α-subunits (Gα), acting as a guanine nucleotide exchange factor and a chaperone. We report two crystal structures of Ric8A, one in the apo form and the other in complex with a tagged C-terminal fragment of Gα. These structures reveal two principal domains of Ric8A: an armadillo-fold core and a flexible C-terminal tail. Additionally, they show that the Gα C-terminus binds to a highly-conserved patch on the concave surface of the Ric8A armadillo-domain, with selectivity determinants residing in the Gα sequence. Biochemical analysis shows that the Ric8A C-terminal tail is critical for its stability and function. A model of the Ric8A/Gα complex derived from crosslinking mass spectrometry and molecular dynamics simulations suggests that the Ric8A C-terminal tail helps organize the GTP-binding site of Gα. This study lays the groundwork for understanding Ric8A function at the molecular level.

PubMed: 31300652
DOI: 10.1038/s41467-019-11088-x

Experimental method

X-RAY DIFFRACTION (1.75 Å)