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-Structure paper
タイトル | Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. |
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ジャーナル・号・ページ | Structure, Vol. 24, Issue 8, Page 1322-1334, Year 2016 |
掲載日 | 2016年8月2日 |
著者 | Masahiko Yamagishi / Hideki Shigematsu / Takeshi Yokoyama / Masahide Kikkawa / Mitsuhiro Sugawa / Mari Aoki / Mikako Shirouzu / Junichiro Yajima / Ryo Nitta / |
PubMed 要旨 | Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is ...Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is unclear how swinging of the neck helix is driven by ATP hydrolysis utilizing the highly conserved catalytic core among all kinesins. Here, using a motility assay, we show that in addition to the neck helix, the conserved five residues at the C-terminal region in kinesin-14, namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its directionality toward the minus end of microtubules. Our structural analyses further demonstrate that the C-terminal neck mimic, in cooperation with conformational changes in the catalytic core during ATP binding, forms a kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end of microtubules. Thus, the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14. |
リンク | Structure / PubMed:27452403 |
手法 | EM (らせん対称) |
解像度 | 5.8 - 6.6 Å |
構造データ | EMDB-8058, PDB-5hnw: EMDB-8059, PDB-5hnx: |
化合物 | ChemComp-MG: ChemComp-GTP: ChemComp-GDP: ChemComp-TA1: ChemComp-ANP: |
由来 |
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キーワード | TRANSPORT PROTEIN / kinesin / kinesin-14 / microtubule / ATPase / STRUCTURAL PROTEIN/MOTOR PROTEIN / STRUCTURAL PROTEIN-MOTOR PROTEIN complex |