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-Structure paper
タイトル | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule. |
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ジャーナル・号・ページ | Elife, Vol. 8, Year 2019 |
掲載日 | 2019年7月2日 |
![]() | Samuel E Lacey / Shaoda He / Sjors Hw Scheres / Andrew P Carter / ![]() |
PubMed 要旨 | Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain ...Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule. |
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手法 | EM (単粒子) |
解像度 | 4.1 - 4.5 Å |
構造データ | EMDB-10060, PDB-6rza: EMDB-10061, PDB-6rzb: |
化合物 | ![]() ChemComp-GTP: ![]() ChemComp-MG: ![]() ChemComp-GDP: ![]() ChemComp-TA1: |
由来 |
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![]() | MOTOR PROTEIN / filament / complex |