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6E88

Cryo-EM structure of C. elegans GDP-microtubule

Summary for 6E88
Entry DOI10.2210/pdb6e88/pdb
EMDB information9004
DescriptorTubulin alpha-2 chain, Tubulin beta-2 chain, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
Functional Keywordscytoskeletal protein, structural protein
Biological sourceCaenorhabditis elegans
More
Total number of polymer chains12
Total formula weight583667.87
Authors
Chaaban, S.,Jariwala, S.,Chieh-Ting, H.,Redemann, S.,Kollman, J.,Muller-Reichert, T.,Sept, D.,Bui, K.H.,Brouhard, G.J. (deposition date: 2018-07-27, release date: 2018-10-10, Last modification date: 2024-03-13)
Primary citationChaaban, S.,Jariwala, S.,Hsu, C.T.,Redemann, S.,Kollman, J.M.,Muller-Reichert, T.,Sept, D.,Bui, K.H.,Brouhard, G.J.
The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth.
Dev. Cell, 47:191-, 2018
Cited by
PubMed Abstract: The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what limits microtubule growth, what determines microtubule structure, or whether the mechanisms of dynamic instability are universal. Here, we studied microtubules from the nematode C. elegans, which have strikingly fast growth rates and non-canonical lattices in vivo. Using a reconstitution approach, we discovered that C. elegans microtubules combine intrinsically fast growth with very frequent catastrophes. We solved the structure of C. elegans microtubules to 4.8 Å and discovered sequence divergence in the lateral contact loops, one of which is ordered in C. elegans but unresolved in other species. We provide direct evidence that C. elegans tubulin has a higher free energy in solution and propose a model wherein the ordering of lateral contact loops activates tubulin for growth.
PubMed: 30245157
DOI: 10.1016/j.devcel.2018.08.023
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.8 Å)
Structure validation

237735

数据于2025-06-18公开中

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