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Ndc80 Kinetochore Complex Structure Data

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Ndc80 Kinetochore Complex Structure Data

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The Ndc80 kinetochore complex forms oligomeric arrays along microtubules

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.

Data description

Linked to the right is a stack (731 MB) of 1,299 helical segments (Spider format) of Ndc80/microtubule complex ([1]) collected at 200 kV and a nominal magnification of 51,200, giving a pixel size on the specimen of 2.48 Å. Alignment parameters determined by Frealign for each segment in the stack can also be found below, as well as a reconstruction of the complex (also Spider format). Run the attached script to recalculate the reconstruction from the image stack and alignment parameters. 
An amplitude scaled version of the map is also available.

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