4FFB

A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule Polymerase

Summary for 4FFB

• Entry DOI: 10.2210/pdb4ffb/pdb
• Descriptor: Tubulin alpha-1 chain, Tubulin beta chain, Protein STU2, ... (5 entities in total)
• Functional Keywords: tubulin fold, heat repeats, cytoskeleton, microtubule, tubulin, tog domain, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm, cytoskeleton: P09733 P02557; Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body: P46675
• Total number of polymer chains: 3
• Total formula weight: 134525.50

Authors

Ayaz, P.,Ye, X.,Huddleston, P.,Brautigam, C.A.,Rice, L.M. (deposition date: 2012-05-31, release date: 2012-08-15, Last modification date: 2023-09-13)

Primary citation

Ayaz, P.,Ye, X.,Huddleston, P.,Brautigam, C.A.,Rice, L.M.
A TOG: alpha beta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.
Science, 337:857-860, 2012

PubMed Abstract: Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use αβ-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of αβ-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 αβ-tubulin. TOG1 binds αβ-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of αβ-tubulin that cannot be incorporated into microtubules, contacting α- and β-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with αβ-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin and how they selectively recognize the growing end of the microtubule.

PubMed: 22904013
DOI: 10.1126/science.1221698

Experimental method

X-RAY DIFFRACTION (2.882 Å)