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Zeng, B.* ; Mou, T.C.* ; Doukov, T.I.* ; Steiner, A. ; Yu, W.* ; Papasergi-Scott, M.* ; Tall, G.G.* ; Hagn, F. ; Sprang, S.R.*

Structure, function, and dynamics of the G alpha binding domain of Ric-8A.

Structure 27, 1137-1147.e5 (2019)
Verlagsversion Preprint Forschungsdaten DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Ric-8A is a 530-amino acid cytoplasmic molecular chaperone and guanine nucleotide exchange factor (GEF) for i, q, and 12/13 classes of heterortrimeric G protein alpha subunits (G alpha). We report the 2.2-angstrom crystal structure of the Ric-8A G alpha-binding domain with GEF activity, residues 1-452, and is phosphorylated at Ser435 and Thr440. Residues 1-429 adopt a superhelical fold comprised of Armadillo (ARM) and HEAT repeats, and the C terminus is disordered. One of the phosphorylated residues potentially binds to a basic cluster in an ARM motif. Amino acid sequence conservation and published hydrogen- deuterium exchange data indicate repeats 3 through 6 to be a putative G alpha-binding surface. Normal mode modeling of small-angle X-ray scattering data indicates that phosphorylation induces relative rotation between repeats 1-4, 5-6, and 7-9. 2D H-1-N-1(5)-TROSY spectra of [H-2, N-15]-labeled Gail in the presence of R452 reveals chemical shift perturbations of the C terminus and Gail residues involved in nucleotide binding.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Guanine Nucleotide Exchange Factor ; Heteronuclear Nuclear Magnetic Resonance ; Heterotrimeric G Protein ; Molecular Chaperone ; Protein Dynamics ; Protein Structure ; Small-angle X-ray Scattering ; X-ray Crystallography; Heterotrimeric G-proteins; Small-angle Scattering; Evolutionary Conservation; Structure Refinement; Structure Validation; Synembryn; Subunit; Molprobity; Software; Insights
ISSN (print) / ISBN 0969-2126
e-ISSN 1878-4186
Zeitschrift Structure
Quellenangaben Band: 27, Heft: 7, Seiten: 1137-1147.e5 Artikelnummer: , Supplement: ,
Verlag Cell Press
Verlagsort 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Begutachtungsstatus Peer reviewed