3IZ0

Human Ndc80 Bonsai Decorated Microtubule

Summary for 3IZ0

• Entry DOI: 10.2210/pdb3iz0/pdb
• EMDB information: 5223
• Descriptor: alpha tubulin, Chain A from PDB 1JFF, beta tubulin, Chain B from PDB 1JFF, NDC80-SPC25 chimera protein, Chain B from PDB 2VE7 (Ndc80 bonsai), ... (9 entities in total)
• Functional Keywords: ndc80, hec1, nuf2, tubulin, kinetochore, mitosis, calponin homology domain, microtubule, cell cycle
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 232614.44

Authors

Alushin, G.M.,Ramey, V.H.,Pasqualato, S.,Ball, D.A.,Grigorieff, N.,Musacchio, A.,Nogales, E. (deposition date: 2010-08-09, release date: 2010-10-13, Last modification date: 2024-02-21)

Primary citation

Alushin, G.M.,Ramey, V.H.,Pasqualato, S.,Ball, D.A.,Grigorieff, N.,Musacchio, A.,Nogales, E.
The Ndc80 kinetochore complex forms oligomeric arrays along microtubules.
Nature, 467:805-810, 2010

PubMed Abstract: The Ndc80 complex is a key site of regulated kinetochore-microtubule attachment (a process required for cell division), but the molecular mechanism underlying its function remains unknown. Here we present a subnanometre-resolution cryo-electron microscopy reconstruction of the human Ndc80 complex bound to microtubules, sufficient for precise docking of crystal structures of the component proteins. We find that the Ndc80 complex binds the microtubule with a tubulin monomer repeat, recognizing α- and β-tubulin at both intra- and inter-tubulin dimer interfaces in a manner that is sensitive to tubulin conformation. Furthermore, Ndc80 complexes self-associate along protofilaments through interactions mediated by the amino-terminal tail of the NDC80 protein, which is the site of phospho-regulation by Aurora B kinase. The complex's mode of interaction with the microtubule and its oligomerization suggest a mechanism by which Aurora B could regulate the stability of load-bearing kinetochore-microtubule attachments.

PubMed: 20944740
DOI: 10.1038/nature09423

Experimental method

ELECTRON MICROSCOPY (8.6 Å)