8IXA

GMPCPP-Alpha1A/Beta2A-microtubule decorated with kinesin non-seam region

Summary for 8IXA

• Entry DOI: 10.2210/pdb8ixa/pdb
• EMDB information: 35790
• Descriptor: Tubulin alpha-1A chain, Tubulin beta-2A chain, Kinesin-1 heavy chain, ... (6 entities in total)
• Functional Keywords: microtubule, tubulin isotype, cryo-em structure, structural protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 27
• Total formula weight: 1308968.24

Authors

Zheng, W.,Zhao, Q.Y.,Diao, L.,Bao, L.,Cong, Y. (deposition date: 2023-03-31, release date: 2023-08-16, Last modification date: 2023-10-25)

Primary citation

Diao, L.,Zheng, W.,Zhao, Q.,Liu, M.,Fu, Z.,Zhang, X.,Bao, L.,Cong, Y.
Cryo-EM of alpha-tubulin isotype-containing microtubules revealed a contracted structure of alpha 4A/ beta 2A microtubules.
Acta Biochim.Biophys.Sin., 55:1551-1560, 2023

PubMed Abstract: Microtubules are hollow α/β-tubulin heterodimeric polymers that play critical roles in cells. In vertebrates, both α- and β-tubulins have multiple isotypes encoded by different genes, which are intrinsic factors in regulating microtubule functions. However, the structures of microtubules composed of different tubulin isotypes, especially α-tubulin isotypes, remain largely unknown. Here, we purify recombinant tubulin heterodimers composed of different mouse α-tubulin isotypes, including α1A, α1C and α4A, with the β-tubulin isotype β2A. We further assemble and determine the cryo-electron microscopy (cryo-EM) structures of α1A/β2A, α1C/β2A, and α4A/β2A microtubules. Our structural analysis demonstrates that α4A/β2A microtubules exhibit longitudinal contraction between tubulin interdimers compared with α1A/β2A and α1C/β2A microtubules. Collectively, our findings reveal that α-tubulin isotype composition can tune microtubule structures, and also provide evidence for the "tubulin code" hypothesis.

PubMed: 37439022
DOI: 10.3724/abbs.2023130

Experimental method

ELECTRON MICROSCOPY (4.2 Å)