Fig. 1: Molecular architecture of the γ-TuSC from C. albicans. | Nature Communications

Fig. 1: Molecular architecture of the γ-TuSC from C. albicans.

From: The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

Fig. 1

a Cryo-EM reconstruction of the γ-TuSC from C. albicans. Segmented cryo-EM densities for Spc97 (green), Spc98 (blue), and γ-tubulins (yellow, orange) are shown. Unassigned density is depicted in gray. The asterisk indicates the γ-tubulin nucleotide-binding pocket shown in panel e. b Atomic model of the γ-TuSC. Dimensions of the complex are given. Coloring as in a. c Atomic model of the Spc97-γ-tubulin heterodimer. The Spc97 model is colored from blue (N-terminus) to red (C-terminus). The location of the missing Spc97 N-terminus is indicated (black circle). The γ-tubulin model is shown in gray and α-helices α6 and α7 are annotated. d Helices α6 and α7 of γ-tubulin (yellow), ‘straight’ β-tubulin (green) and ‘curved’ β-tubulin (magenta) superposed to the cryo-EM density of Spc97-associated γ-tubulin. e Atomic model for GDP (cyan) superposed to cryo-EM density (gray) in the nucleotide-binding pocket of Spc97-associated γ-tubulin (yellow). The density does not indicate the presence of a γ-phosphate group. Zoom as indicated by the asterisk in panel a.

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