5MJS

S. pombe microtubule copolymerized with GTP and Mal3-143

5MJS の概要

• エントリーDOI: 10.2210/pdb5mjs/pdb
• EMDBエントリー: 3522
• 分子名称: Tubulin beta chain, Microtubule integrity protein mal3, Tubulin alpha-1 chain, ... (5 entities in total)
• 機能のキーワード: schizosaccharomyces pombe microtubules, structural protein
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 408553.88

構造登録者

von Loeffelholz, O.,Moores, C. (登録日: 2016-12-01, 公開日: 2017-12-20, 最終更新日: 2019-10-23)

主引用文献

von Loeffelholz, O.,Venables, N.A.,Drummond, D.R.,Katsuki, M.,Cross, R.,Moores, C.A.
Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics.
Nat Commun, 8:2110-2110, 2017

PubMed Abstract: Using cryo-electron microscopy, we characterize the architecture of microtubules assembled from Schizosaccharomyces pombe tubulin, in the presence and absence of their regulatory partner Mal3. Cryo-electron tomography reveals that microtubules assembled from S. pombe tubulin have predominantly B-lattice interprotofilament contacts, with protofilaments skewed around the microtubule axis. Copolymerization with Mal3 favors 13 protofilament microtubules with reduced protofilament skew, indicating that Mal3 adjusts interprotofilament interfaces. A 4.6-Å resolution structure of microtubule-bound Mal3 shows that Mal3 makes a distinctive footprint on the S. pombe microtubule lattice and that unlike mammalian microtubules, S. pombe microtubules do not show the longitudinal lattice compaction associated with EB protein binding and GTP hydrolysis. Our results firmly support a structural plasticity view of microtubule dynamics in which microtubule lattice conformation is sensitive to a variety of effectors and differently so for different tubulins.

PubMed: 29235477
DOI: 10.1038/s41467-017-02241-5

実験手法

ELECTRON MICROSCOPY (4.6 Å)