Structural highlights
Function
TBA1_YEAST Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
Publication Abstract from PubMed
Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use alphabeta-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of alphabeta-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast alphabeta-tubulin. TOG1 binds alphabeta-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of alphabeta-tubulin that cannot be incorporated into microtubules, contacting alpha- and beta-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with alphabeta-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of alphabeta-tubulin and how they selectively recognize the growing end of the microtubule.
A TOG:alphabeta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.,Ayaz P, Ye X, Huddleston P, Brautigam CA, Rice LM Science. 2012 Aug 17;337(6096):857-60. PMID:22904013[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ayaz P, Ye X, Huddleston P, Brautigam CA, Rice LM. A TOG:alphabeta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. Science. 2012 Aug 17;337(6096):857-60. PMID:22904013 doi:10.1126/science.1221698
