A tethered delivery mechanism explains the catalytic action of a microtubule polymerase

A tethered delivery mechanism explains the catalytic action of a microtubule polymerase

Stu2p/XMAP215 proteins are essential microtubule polymerases that use multiple αβ-tubulin-interacting TOG domains to bind microtubule plus ends and catalyze fast microtubule growth. We report here the structure of the TOG2 domain from Stu2p bound to yeast αβ-tubulin. Like TOG1, TOG2 binds selectivel...

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Bibliographic Details
Main Authors: Pelin Ayaz, Sarah Munyoki, Elisabeth A Geyer, Felipe-Andrés Piedra, Emily S Vu, Raquel Bromberg, Zbyszek Otwinowski, Nick V Grishin, Chad A Brautigam, Luke M Rice
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2014-08-01
Series:eLife
Subjects:
microtubule
TOG domain
kinetic simulation
X-ray structure
conformation-selective
Online Access:https://elifesciences.org/articles/03069

Internet

https://elifesciences.org/articles/03069

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