PDBsum entry 6o2r

Structural protein

PDB id: 6o2r

Contents

Protein chains

(+ 0 more) 432 a.a.

(+ 0 more) 429 a.a.

Ligands

GTP ×6

GDP ×6

Metals

_MG ×6

PDB id:

6o2r

Name:

Structural protein

Title:

Deacetylated microtubules

Structure:

Tubulin alpha-1b chain. Chain: a, c, e, j, k, l. Synonym: alpha-tubulin ubiquitous, tubulin k-alpha-1, tubulin alpha- ubiquitous chain. Tubulin beta chain. Chain: b, d, f, g, h, i. Synonym: beta-tubulin

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Tissue: brain. Tissue: brain

Authors:

L.Eshun-Wilson,R.Zhang,D.Portran,M.V.Nachury,D.Toso,T.Lohr, M.Vendruscolo,M.Bonomi,J.S.Fraser,E.Nogales

Key ref:

L.Eshun-Wilson et al. (2019). Effects of α-tubulin acetylation on microtubule structure and stability. Proc Natl Acad Sci U S A, 116, 10366-10371. PubMed id: 31072936 DOI: 10.1073/pnas.1900441116

Date:

24-Feb-19 Release date: 22-May-19

Protein chains

Q2XVP4  (TBA1B_PIG) -  Tubulin alpha-1B chain from Sus scrofa

Seq: 451 a.a.

Struc: 432 a.a.

Protein chains

P02554  (TBB_PIG) -  Tubulin beta chain from Sus scrofa

Seq: 445 a.a.

Struc: 429 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, C, E, J, K, L: E.C.3.6.5.- - ?????
• Enzyme class 2: Chains B, D, F, G, H, I: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1073/pnas.1900441116

Proc Natl Acad Sci U S A 116:10366-10371 (2019)

PubMed id: 31072936

Effects of α-tubulin acetylation on microtubule structure and stability.

L.Eshun-Wilson, R.Zhang, D.Portran, M.V.Nachury, D.B.Toso, T.Löhr, M.Vendruscolo, M.Bonomi, J.S.Fraser, E.Nogales.

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.