Fig. 4: The C. albicans γ-TuSC requires conformational rearrangements during or after oligomerization. | Nature Communications

Fig. 4: The C. albicans γ-TuSC requires conformational rearrangements during or after oligomerization.

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

Fig. 4

Atomic models for the C. albicans (a, gray) and vertebrate (b, gray) γ-TuSC units were superposed to the S. cerevisiae γ-TuSC in the closed conformation (colored) according to the first spoke (Spc97/GCP2 plus γ-tubulin). The displacement of domains was visualized by trajectories linking the backbone atoms in the two superposed models. For orientation, atomic models for the first spoke are superposed to trajectories. Trajectories are color-coded from low (blue) to high (red) motion. In the ‘top view’, arrows representing the average direction and magnitude of γ-tubulin displacement are superposed to the trajectories.

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