3J7I

Structure of alpha- and beta- tubulin in GMPCPP-microtubules

Summary for 3J7I

• Entry DOI: 10.2210/pdb3j7i/pdb
• EMDB information: 2697
• Descriptor: Tubulin alpha-1A chain, Tubulin beta chain, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: microtubule, tubulin, gtp-state structure, gmpcpp, microtubule stabilaization, micotubule polymerization, structural protein
• Biological source: Sus scrofa (pig); More
• Total number of polymer chains: 2
• Total formula weight: 101109.98

Authors

Yajima, H.,Ogura, T.,Nitta, R.,Okada, Y.,Sato, C.,Hirokawa, N. (deposition date: 2014-07-01, release date: 2014-12-10, Last modification date: 2024-03-20)

Primary citation

Yajima, H.,Ogura, T.,Nitta, R.,Okada, Y.,Sato, C.,Hirokawa, N.
Conformational changes in tubulin in GMPCPP and GDP-taxol microtubules observed by cryoelectron microscopy
J.Cell Biol., 198:315-322, 2012

PubMed Abstract: Microtubules are dynamic polymers that stochastically switch between growing and shrinking phases. Microtubule dynamics are regulated by guanosine triphosphate (GTP) hydrolysis by β-tubulin, but the mechanism of this regulation remains elusive because high-resolution microtubule structures have only been revealed for the guanosine diphosphate (GDP) state. In this paper, we solved the cryoelectron microscopy (cryo-EM) structure of microtubule stabilized with a GTP analogue, guanylyl 5'-α,β-methylenediphosphonate (GMPCPP), at 8.8-Å resolution by developing a novel cryo-EM image reconstruction algorithm. In contrast to the crystal structures of GTP-bound tubulin relatives such as γ-tubulin and bacterial tubulins, significant changes were detected between GMPCPP and GDP-taxol microtubules at the contacts between tubulins both along the protofilament and between neighboring protofilaments, contributing to the stability of the microtubule. These findings are consistent with the structural plasticity or lattice model and suggest the structural basis not only for the regulatory mechanism of microtubule dynamics but also for the recognition of the nucleotide state of the microtubule by several microtubule-binding proteins, such as EB1 or kinesin.

PubMed: 22851320
DOI: 10.1083/jcb.201201161

Experimental method

ELECTRON MICROSCOPY (8.9 Å)