6O2R
Deacetylated Microtubules
Summary for 6O2R
Entry DOI | 10.2210/pdb6o2r/pdb |
EMDB information | 0612 0613 0614 0615 |
Descriptor | Tubulin alpha-1B chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
Functional Keywords | microtubule, cytoskeleton, acetylation, structural protein |
Biological source | Sus scrofa (Pig) More |
Total number of polymer chains | 12 |
Total formula weight | 606617.41 |
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 citation | Eshun-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: 31072936DOI: 10.1073/pnas.1900441116 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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