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-Structure paper
タイトル | Structural basis for two-way communication between dynein and microtubules. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 1038, Year 2020 |
掲載日 | 2020年2月25日 |
著者 | Noritaka Nishida / Yuta Komori / Osamu Takarada / Atsushi Watanabe / Satoko Tamura / Satoshi Kubo / Ichio Shimada / Masahide Kikkawa / |
PubMed 要旨 | The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but ...The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk α-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk α-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks. |
リンク | Nat Commun / PubMed:32098965 / PubMed Central |
手法 | EM (らせん対称) / NMR (溶液) |
解像度 | 3.62 - 3.94 Å |
構造データ | EMDB-9996, PDB-6kio: EMDB-9997, PDB-6kiq: PDB-6kjn: PDB-6kjo: |
由来 |
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キーワード | MOTOR PROTEIN/STRUCTURAL PROTEIN / MOTOR PROTEIN-STRUCTURAL PROTEIN COMPLEX / Dynein / Microtubule / MOTOR PROTEIN / disulfide bond / high affinity / low affinity |