7M3P

Xrcc4-Spc110p(164-207) fusion

Summary for 7M3P

• Entry DOI: 10.2210/pdb7m3p/pdb
• EMDB information: 23635 23636 23637 23638 23639
• Descriptor: Xrcc4-Spc110p(164-207) (2 entities in total)
• Functional Keywords: microtubule nucleation, cell cycle
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 41466.43

Authors

Brilot, A.F.,Lyon, A.S.,Zelter, A.,Viswanath, S.,Maxwell, A.,MacCoss, M.J.,Muller, E.G.,Sali, A.,Davis, T.N.,Agard, D.A. (deposition date: 2021-03-18, release date: 2021-05-12, Last modification date: 2023-10-18)

Primary citation

Brilot, A.F.,Lyon, A.S.,Zelter, A.,Viswanath, S.,Maxwell, A.,MacCoss, M.J.,Muller, E.G.,Sali, A.,Davis, T.N.,Agard, D.A.
CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation.
Elife, 10:-, 2021

PubMed Abstract: Microtubule (MT) nucleation is regulated by the γ-tubulin ring complex (γTuRC), conserved from yeast to humans. In , γTuRC is composed of seven identical γ-tubulin small complex (γTuSC) sub-assemblies, which associate helically to template MT growth. γTuRC assembly provides a key point of regulation for the MT cytoskeleton. Here, we combine crosslinking mass spectrometry, X-ray crystallography, and cryo-EM structures of both monomeric and dimeric γTuSCs, and open and closed helical γTuRC assemblies in complex with Spc110p to elucidate the mechanisms of γTuRC assembly. γTuRC assembly is substantially aided by the evolutionarily conserved CM1 motif in Spc110p spanning a pair of adjacent γTuSCs. By providing the highest resolution and most complete views of any γTuSC assembly, our structures allow phosphorylation sites to be mapped, surprisingly suggesting that they are mostly inhibitory. A comparison of our structures with the CM1 binding site in the human γTuRC structure at the interface between GCP2 and GCP6 allows for the interpretation of significant structural changes arising from CM1 helix binding to metazoan γTuRC.

PubMed: 33949948
DOI: 10.7554/eLife.65168

Experimental method

X-RAY DIFFRACTION (2.00001856449 Å)