Fig. 1: Cryo-ET imaging of pericentriolar γ-TuRCs identifies a novel binding site for γ-TuRC interactors. | Nature Communications

Fig. 1: Cryo-ET imaging of pericentriolar γ-TuRCs identifies a novel binding site for γ-TuRC interactors.

From: Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC

Fig. 1

a Three-dimensional rendering of a cryo-electron tomogram depicting a centrosome purified from human KE37 cells. Microtubule triplets (MTTs) and identified γ-TuRCs are annotated in green and yellow, respectively. b Cryo-EM density of the human γ-TuRC from purified centrosomes at 16.4 Å resolution. The atomic model of the recombinant human γ-TuRC was superposed (PDB: 7QJ57; N-GCP3/MZT1 and N-GCP5/MZT1 not shown). Coloring as indicated; box indicates density segment not previously observed on the γ-TuRC. c AlphaFold2 prediction for the tetrameric NEDD1C/N-GCP3/MZT1 complex (disordered regions not shown). The tetrameric NEDD1C coiled coil is surrounded by four symmetrically arranged N-GCP3/MZT1 modules. Coloring as indicated. d AlphaFold2 model from (c), rigid body-docked into the density segment from (b).

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