6UGD

Katanin hexamer in the spiral conformation in complex with substrate

6UGD の概要

• エントリーDOI: 10.2210/pdb6ugd/pdb
• EMDBエントリー: 20761
• 分子名称: Meiotic spindle formation protein mei-1, Polyglutamate peptide, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: katanin, microtubule-severing, mei-1, microtubule cytoskeleton, motor protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 326448.24

構造登録者

Zehr, E.A.,Roll-Mecak, A. (登録日: 2019-09-26, 公開日: 2019-10-09, 最終更新日: 2024-03-20)

主引用文献

Zehr, E.A.,Szyk, A.,Szczesna, E.,Roll-Mecak, A.
Katanin Grips the beta-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.
Dev.Cell, 52:118-131.e6, 2020

PubMed Abstract: The AAA ATPase katanin severs microtubules. It is critical in cell division, centriole biogenesis, and neuronal morphogenesis. Its mutation causes microcephaly. The microtubule templates katanin hexamerization and activates its ATPase. The structural basis for these activities and how they lead to severing is unknown. Here, we show that β-tubulin tails are necessary and sufficient for severing. Cryoelectron microscopy (cryo-EM) structures reveal the essential tubulin tail glutamates gripped by a double spiral of electropositive loops lining the katanin central pore. Each spiral couples allosterically to the ATPase and binds alternating, successive substrate residues, with consecutive residues coordinated by adjacent protomers. This tightly couples tail binding, hexamerization, and ATPase activation. Hexamer structures in different states suggest an ATPase-driven, ratchet-like translocation of the tubulin tail through the pore. A disordered region outside the AAA core anchors katanin to the microtubule while the AAA motor exerts the forces that extract tubulin dimers and sever the microtubule.

PubMed: 31735665
DOI: 10.1016/j.devcel.2019.10.010

実験手法

ELECTRON MICROSCOPY (3.5 Å)