4UBF

HsMCAK motor domain complex

4UBF の概要

• エントリーDOI: 10.2210/pdb4ubf/pdb
• 分子名称: Kinesin-like protein KIF2C, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: mcak, kif2c, complex, motor domain, cell cycle
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 176437.80

構造登録者

Welburn, J.P.I.,Talapatra, S.K. (登録日: 2014-08-12, 公開日: 2015-05-06, 最終更新日: 2023-12-20)

主引用文献

Talapatra, S.K.,Harker, B.,Welburn, J.P.
The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch.
Elife, 4:-, 2015

PubMed Abstract: The precise regulation of microtubule dynamics is essential during cell division. The kinesin-13 motor protein MCAK is a potent microtubule depolymerase. The divergent non-motor regions flanking the ATPase domain are critical in regulating its targeting and activity. However, the molecular basis for the function of the non-motor regions within the context of full-length MCAK is unknown. Here, we determine the structure of MCAK motor domain bound to its regulatory C-terminus. Our analysis reveals that the MCAK C-terminus binds to two motor domains in solution and is displaced allosterically upon microtubule binding, which allows its robust accumulation at microtubule ends. These results demonstrate that MCAK undergoes long-range conformational changes involving its C-terminus during the soluble to microtubule-bound transition and that the C-terminus-motor interaction represents a structural intermediate in the MCAK catalytic cycle. Together, our work reveals intrinsic molecular mechanisms underlying the regulation of kinesin-13 activity.

PubMed: 25915621
DOI: 10.7554/eLife.06421

実験手法

X-RAY DIFFRACTION (3 Å)