7ANZ

Structure of the Candida albicans gamma-Tubulin Small Complex

Summary for 7ANZ

• Entry DOI: 10.2210/pdb7anz/pdb
• EMDB information: 11835
• Descriptor: Tubulin gamma chain, Spindle pole body component (3 entities in total)
• Functional Keywords: gamma-tubulin small complex, cytoskeleton, microtubule nucleation, cytosolic protein
• Biological source: Candida albicans; More
• Total number of polymer chains: 4
• Total formula weight: 307021.72

Authors

Zupa, E.,Pfeffer, S. (deposition date: 2020-10-13, release date: 2020-11-04, Last modification date: 2024-05-01)

Primary citation

Zupa, E.,Zheng, A.,Neuner, A.,Wurtz, M.,Liu, P.,Bohler, A.,Schiebel, E.,Pfeffer, S.
The cryo-EM structure of a gamma-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.
Nat Commun, 11:5705-5705, 2020

PubMed Abstract: The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is achieved and regulated by a minimal microtubule nucleation system, we here determined the cryo-electron microscopy structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. Compared to the vertebrate γ-tubulin ring complex (γ-TuRC), we observed a vastly remodeled interface between the SPC/GCP-γ-tubulin spokes, which stabilizes the complex and defines the γ-tubulin arrangement. The relative positioning of γ-tubulin subunits indicates that a conformational rearrangement of the complex is required for microtubule nucleation activity, which follows opposing directionality as predicted for the vertebrate γ-TuRC. Collectively, our data suggest that the assembly and regulation mechanisms of γ-tubulin complexes fundamentally differ between the microtubule nucleation systems in lower and higher eukaryotes.

PubMed: 33177498
DOI: 10.1038/s41467-020-19456-8

Experimental method

ELECTRON MICROSCOPY (3.6 Å)