2RPA

The solution structure of N-terminal domain of microtubule severing enzyme

2RPA の概要

• エントリーDOI: 10.2210/pdb2rpa/pdb
• 分子名称: Katanin p60 ATPase-containing subunit A1 (1 entity in total)
• 機能のキーワード: aaa atpase, atp-binding, cell cycle, cell division, cytoplasm, hydrolase, microtubule, microtubule severing enzyme, mitosis, nucleotide-binding
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm (By similarity): Q9WV86
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9256.64

構造登録者

Iwaya, N.,Kuwahara, Y.,Unzai, S.,Nagata, T.,Tomii, K.,Goda, N.,Tochio, H.,Shirakawa, M.,Hiroaki, H. (登録日: 2008-05-13, 公開日: 2009-05-26, 最終更新日: 2024-05-29)

主引用文献

Iwaya, N.,Kuwahara, Y.,Fujiwara, Y.,Goda, N.,Tenno, T.,Akiyama, K.,Mase, S.,Tochio, H.,Ikegami, T.,Shirakawa, M.,Hiroaki, H.
A common substrate recognition mode conserved between katanin P60 and VPS4 governs microtubule severing and membrane skeleton reorganization
J.Biol.Chem., 285:16822-16829, 2010

PubMed Abstract: Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD was determined by NMR. Although their sequence similarities were as low as 20%, the structure of kp60-NTD revealed a striking similarity to those of the microtubule interacting and trafficking (MIT) domains, which adopt anti-parallel three-stranded helix bundle. In particular, the arrangement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, which is a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. Mutation studies revealed that the positively charged surface formed by helices 2 and 3 binds tubulin. This binding mode resembles the interaction between the MIT domain of Vps4 and Vps2/CHMP1a, a component of endosomal sorting complexes required for transport III. Our results show that both the molecular architecture and the binding modes are conserved between two AAA-ATPases, kp60 and Vps4. A common mechanism is evolutionarily conserved between two distinct cellular events, one that drives microtubule severing and the other involving membrane skeletal reorganization.

PubMed: 20339000
DOI: 10.1074/jbc.M110.108365

実験手法

SOLUTION NMR