Fig. 2: Conformational changes and interactions involved in γ-TuSC oligomerisation. | Nature Communications

Fig. 2: Conformational changes and interactions involved in γ-TuSC oligomerisation.

From: Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors

Fig. 2

a The C-terminal parts of Spc97/98 GRIP1 domains (GRIP1C), full GRIP2 domains and γ-tubulins undergo a hinge motion relative to the N-terminal part of the GRIP1 (GRIP1N) domain upon γ-TuSC oligomerisation. Colouring scheme is indicated at the bottom of panel (b). b During the conformational change shown in panel (a), the γ-tubulin molecules move closer together (top view). Models were superposed on the GRIP1C/GRIP2 domain of Spc97 with γ-tubulin. c Remodeling of the extended interface between GRIP2 domains upon oligomerisation. Colouring as indicated in panel (b). d Electrostatic interactions at the interface between two γ-tubulin molecules in the oligomeric γ-TuSC. e Docking of Spc97 Phe721 in a strongly hydrophobic pocket of Spc98 in the neighbouring γ-TuSC.

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