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PDBsum entry 6o2r
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Structural protein
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PDB id
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6o2r
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Contents |
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(+ 0 more)
432 a.a.
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(+ 0 more)
429 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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Effects of α-Tubulin acetylation on microtubule structure and stability.
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Authors
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L.Eshun-Wilson,
R.Zhang,
D.Portran,
M.V.Nachury,
D.B.Toso,
T.Löhr,
M.Vendruscolo,
M.Bonomi,
J.S.Fraser,
E.Nogales.
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Ref.
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Proc Natl Acad Sci U S A, 2019,
116,
10366-10371.
[DOI no: ]
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PubMed id
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Abstract
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Acetylation of K40 in α-tubulin is the sole posttranslational modification to
mark the luminal surface of microtubules. It is still controversial whether its
relationship with microtubule stabilization is correlative or causative. We have
obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of
pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to
visualize the structural consequences of this modification and reveal its
potential for influencing the larger assembly properties of microtubules. We
modeled the conformational ensembles of the unmodified and acetylated states by
using the experimental cryo-EM density as a structural restraint in molecular
dynamics simulations. We found that acetylation alters the conformational
landscape of the flexible loop that contains αK40. Modification of αK40
reduces the disorder of the loop and restricts the states that it samples. We
propose that the change in conformational sampling that we describe, at a
location very close to the lateral contacts site, is likely to affect
microtubule stability and function.
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