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6O2R

Deacetylated Microtubules

Summary for 6O2R
Entry DOI10.2210/pdb6o2r/pdb
EMDB information0612 0613 0614 0615
DescriptorTubulin alpha-1B chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
Functional Keywordsmicrotubule, cytoskeleton, acetylation, structural protein
Biological sourceSus scrofa (Pig)
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Total number of polymer chains12
Total formula weight606617.41
Authors
Eshun-Wilson, L.,Zhang, R.,Portran, D.,Nachury, M.V.,Toso, D.,Lohr, T.,Vendruscolo, M.,Bonomi, M.,Fraser, J.S.,Nogales, E. (deposition date: 2019-02-24, release date: 2019-05-22, Last modification date: 2024-03-20)
Primary citationEshun-Wilson, L.,Zhang, R.,Portran, D.,Nachury, M.V.,Toso, D.B.,Lohr, T.,Vendruscolo, M.,Bonomi, M.,Fraser, J.S.,Nogales, E.
Effects of alpha-tubulin acetylation on microtubule structure and stability.
Proc.Natl.Acad.Sci.USA, 116:10366-10371, 2019
Cited by
PubMed Abstract: 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.
PubMed: 31072936
DOI: 10.1073/pnas.1900441116
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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