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PDBsum entry 4ffb
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Contents |
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435 a.a.
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421 a.a.
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231 a.a.
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References listed in PDB file
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Key reference
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Title
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A tog:αβ-Tubulin complex structure reveals conformation-Based mechanisms for a microtubule polymerase.
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Authors
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P.Ayaz,
X.Ye,
P.Huddleston,
C.A.Brautigam,
L.M.Rice.
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Ref.
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Science, 2012,
337,
857-860.
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PubMed id
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Abstract
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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.
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