9QVN

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

これはPDB形式変換不可エントリーです。

9QVN の概要

• エントリーDOI: 10.2210/pdb9qvn/pdb
• EMDBエントリー: 53400
• 分子名称: Gamma-tubulin complex component 3, Mitotic-spindle organizing protein 1, Protein NEDD1, ... (9 entities in total)
• 機能のキーワード: tubulin complex, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 45
• 化学式量合計: 3154192.92

構造登録者

Munoz-Hernandez, H.,Xu, Y.,Wieczorek, M. (登録日: 2025-04-11, 公開日: 2025-05-21, 最終更新日: 2025-06-04)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4.7 Å)