4Y05

KIF2C short Loop2 construct

4Y05 の概要

• エントリーDOI: 10.2210/pdb4y05/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: kinesin-13, microtubule, tubulin, transport protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44173.25

構造登録者

Wang, W.,Knossow, M.,Gigant, B. (登録日: 2015-02-05, 公開日: 2015-06-17, 最終更新日: 2024-01-10)

主引用文献

Wang, W.,Shen, T.,Guerois, R.,Zhang, F.,Kuerban, H.,Lv, Y.,Gigant, B.,Knossow, M.,Wang, C.
New Insights into the Coupling between Microtubule Depolymerization and ATP Hydrolysis by Kinesin-13 Protein Kif2C.
J.Biol.Chem., 290:18721-18731, 2015

PubMed Abstract: Kinesin-13 proteins depolymerize microtubules in an ATP hydrolysis-dependent manner. The coupling between these two activities remains unclear. Here, we first studied the role of the kinesin-13 subfamily-specific loop 2 and of the KVD motif at the tip of this loop. Shortening the loop, the lysine/glutamate interchange and the additional Val to Ser substitution all led to Kif2C mutants with decreased microtubule-stimulated ATPase and impaired depolymerization capability. We rationalized these results based on a structural model of the Kif2C-ATP-tubulin complex derived from the recently determined structures of kinesin-1 bound to tubulin. In this model, upon microtubule binding Kif2C undergoes a conformational change governed in part by the interaction of the KVD motif with the tubulin interdimer interface. Second, we mutated to an alanine the conserved glutamate residue of the switch 2 nucleotide binding motif. This mutation blocks motile kinesins in a post-conformational change state and inhibits ATP hydrolysis. This Kif2C mutant still depolymerized microtubules and yielded complexes of one Kif2C with two tubulin heterodimers. These results demonstrate that the structural change of Kif2C-ATP upon binding to microtubule ends is sufficient for tubulin release, whereas ATP hydrolysis is not required. Overall, our data suggest that the conformation reached by kinesin-13s upon tubulin binding is similar to that of tubulin-bound, ATP-bound, motile kinesins but that this conformation is adapted to microtubule depolymerization.

PubMed: 26055718
DOI: 10.1074/jbc.M115.646919

実験手法

X-RAY DIFFRACTION (2.59 Å)