8SF7

48-nm doublet microtubule from Tetrahymena thermophila strain MEC17

This is a non-PDB format compatible entry.

Summary for 8SF7

• Entry DOI: 10.2210/pdb8sf7/pdb
• Related: 8G2Z 8G3D
• EMDB information: 29666 29667 29685 29692 29693 40436
• Descriptor: Nebulin, CFAP161A, CFAP20, ... (48 entities in total)
• Functional Keywords: cilia, axoneme, doublet microtubule, microtubule inner protein, structural protein
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 431
• Total formula weight: 20338705.62

Authors

Black, C.S.,Kubo, S.,Yang, S.K.,Bui, K.H. (deposition date: 2023-04-10, release date: 2024-05-22, Last modification date: 2024-10-09)

Primary citation

Yang, S.K.,Kubo, S.,Black, C.S.,Peri, K.,Dai, D.,Legal, T.,Valente-Paterno, M.,Gaertig, J.,Bui, K.H.
Effect of alpha-tubulin acetylation on the doublet microtubule structure.
Elife, 12:-, 2024

PubMed Abstract: Acetylation of α-tubulin at the lysine 40 residue (αK40) by αTAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that acetylated microtubules are more stable and damage resistant. αK40 acetylation is the only known microtubule luminal post-translational modification site. The luminal location suggests that the modification tunes the lateral interaction of protofilaments inside the microtubule. In this study, we examined the effect of tubulin acetylation on the doublet microtubule (DMT) in the cilia of using a combination of cryo-electron microscopy, molecular dynamics, and mass spectrometry. We found that αK40 acetylation exerts a small-scale effect on the DMT structure and stability by influencing the lateral rotational angle. In addition, comparative mass spectrometry revealed a link between αK40 acetylation and phosphorylation in cilia.

PubMed: 38598282
DOI: 10.7554/eLife.92219

Experimental method

ELECTRON MICROSCOPY (4.1 Å)