+検索条件
-Structure paper
| タイトル | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule. |
|---|---|
| ジャーナル・号・ページ | Elife, Vol. 8, Year 2019 |
| 掲載日 | 2019年7月2日 |
著者 | 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. |
リンク | Elife / PubMed:31264960 / PubMed Central |
| 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 |
|
キーワード | MOTOR PROTEIN / filament / complex |
ムービー
コントローラー
構造ビューア
万見文献について



著者
リンク







homo sapiens (ヒト)
キーワード