6V6C

Structure of GCP6 in the native human gamma-tubulin ring complex

6V6C の概要

• エントリーDOI: 10.2210/pdb6v6c/pdb
• EMDBエントリー: 21068
• 分子名称: Gamma-tubulin complex component 6 (1 entity in total)
• 機能のキーワード: gcp, gcp6, gamma-tubulin ring complex, gturc, g-turc, microtubule, microtubule nucleation, single particle cryo-em structure, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 200733.64

構造登録者

Wieczorek, M.,Urnavicius, L.,Ti, S.,Molloy, K.R.,Chait, B.T.,Kapoor, T.M. (登録日: 2019-12-04, 公開日: 2020-01-01, 最終更新日: 2025-06-04)

主引用文献

Wieczorek, M.,Urnavicius, L.,Ti, S.C.,Molloy, K.R.,Chait, B.T.,Kapoor, T.M.
Asymmetric Molecular Architecture of the Human gamma-Tubulin Ring Complex.
Cell, 180:165-175.e16, 2020

PubMed Abstract: The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human γ-TuRC at ∼3.8 Å resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the γ-TuRC "seam." We also identify an unanticipated structural bridge that includes an actin-like protein and spans the γ-TuRC lumen. Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the γ-TuRC subunits introduces large (>100,000 Å) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the γ-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments.

PubMed: 31862189
DOI: 10.1016/j.cell.2019.12.007

実験手法

ELECTRON MICROSCOPY (4.5 Å)