9QVN

Cryo-EM reconstruction of the NEDD1 anchor protein bound to the gamma-tubulin ring complex

This is a non-PDB format compatible entry.

Summary for 9QVN

• Entry DOI: 10.2210/pdb9qvn/pdb
• EMDB information: 53400
• Descriptor: Gamma-tubulin complex component 3, Mitotic-spindle organizing protein 1, Protein NEDD1, ... (9 entities in total)
• Functional Keywords: tubulin complex, structural protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 45
• Total formula weight: 3154192.92

Authors

Munoz-Hernandez, H.,Xu, Y.,Wieczorek, M. (deposition date: 2025-04-11, release date: 2025-05-21, Last modification date: 2025-06-04)

Primary citation

Munoz-Hernandez, H.,Xu, Y.,Pellicer Camardiel, A.,Zhang, D.,Xue, A.,Aher, A.,Walker, E.,Marxer, F.,Kapoor, T.M.,Wieczorek, M.
Structure of the microtubule-anchoring factor NEDD1 bound to the gamma-tubulin ring complex.
J.Cell Biol., 224:-, 2025

PubMed Abstract: The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly that provides a template for microtubule nucleation. The γ-TuRC is recruited to microtubule-organizing centers (MTOCs) by the evolutionarily conserved attachment factor NEDD1. However, the structural basis of the NEDD1-γ-TuRC interaction is not known. Here, we report cryo-EM structures of NEDD1 bound to the human γ-TuRC in the absence or presence of the activating factor CDK5RAP2. We found that the C-terminus of NEDD1 forms a tetrameric α-helical assembly that contacts the lumen of the γ-TuRC cone and orients its microtubule-binding domain away from the complex. The structure of the γ-TuRC simultaneously bound to NEDD1 and CDK5RAP2 reveals that both factors can associate with the "open" conformation of the complex. Our results show that NEDD1 does not induce substantial conformational changes in the γ-TuRC but suggest that anchoring of γ-TuRC-capped microtubules by NEDD1 would be structurally compatible with the significant conformational changes experienced by the γ-TuRC during microtubule nucleation.

PubMed: 40396914
DOI: 10.1083/jcb.202410206

Experimental method

ELECTRON MICROSCOPY (4.7 Å)