Fig. 3: Conformation-dependent pattern of CDK5RAP2 CM1 module recruitment. | Nature Communications

Fig. 3: Conformation-dependent pattern of CDK5RAP2 CM1 module recruitment.

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

Fig. 3

a Cryo-EM densities of the inwards (yellow) and outwards (gray) conformations superposed according to GCP GRIP1 domains. b Superposed rigid body-fitted models of the inwards and outwards conformations seen in the top (left) and side view (right). See Supplementary Fig. 9 and Methods for details. Arrows indicate the rigid body motion of GRIP2 domains and γ-tubulins. c Deviation of γ-TuRC geometry from the fully closed MT-capping human γ-TuRC (PDB: 8VRK53). The inwards and outwards conformations of PCM-located human γ-TuRCs, as well as purified recombinant (PDB: 7AS45) and native human γ-TuRCs (PDB: 6V6S4) were analyzed. All models were superposed according to spokes 2–8, and deviations were calculated based on the γ-tubulin centers determined in ChimeraX using the “measure center” command. d Cryo-EM density of a GCP2/3 unit (white) with a stoichiometric additional density segment on the outside of GCP2 (gray). The experimental model of the CDK5RAP2 CM1 module was superposed (PDB: 6V6S4). e Schematic representation of conformation-dependent CDK5RAP2 CM1 module binding for the inwards (yellow) and outwards (gray) conformations (see also Supplementary Fig. 12a). GCP2-containing spokes are indicated in light blue. Source data are provided as a Source Data file.

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