9H9Q
Candida albicans gamma-tubulin small complex within ring-like higher oligomer in complex with Spc72 CM1
Summary for 9H9Q
| Entry DOI | 10.2210/pdb9h9q/pdb |
| Related | 9H9P 9H9R |
| EMDB information | 51971 51972 |
| Descriptor | Tubulin gamma chain, Spindle pole body component, Spc98p, ... (4 entities in total) |
| Functional Keywords | cytoskeleton, microtubule, microtubule nucleation, complex, template, cap, gamma-tubulin, gamma-tubulin ring complex, gamma-tubulin small complex, spc72, cm1, cm1 motif, gcp2, gcp3, spc97, spc98, candida, albicans, cell cycle, gamma-turc, gamma-tusc, yeast, fungi |
| Biological source | Candida albicans More |
| Total number of polymer chains | 12 |
| Total formula weight | 907425.64 |
| Authors | |
| Primary citation | Zheng, A.,Vermeulen, B.J.A.,Wurtz, M.,Neuner, A.,Lubbehusen, N.,Mayer, M.P.,Schiebel, E.,Pfeffer, S. Structural insights into the interplay between microtubule polymerases, gamma-tubulin complexes and their receptors. Nat Commun, 16:402-402, 2025 Cited by PubMed Abstract: The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 Å resolution, revealing how the γ-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal α-helix of Stu2 and thereby position the α/β-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in γ-TuSC oligomerisation and the recruitment of microtubule polymerases to the γ-TuRC. PubMed: 39757296DOI: 10.1038/s41467-024-55778-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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