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| Title | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule. |
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| Journal, issue, pages | Elife, Vol. 8, Year 2019 |
| Publish date | Jul 2, 2019 |
 Authors | Samuel E Lacey / Shaoda He / Sjors Hw Scheres / Andrew P Carter /  |
| PubMed Abstract | 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. |
 External links | Elife / PubMed:31264960 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.1 - 4.5 Å |
| Structure data | EMDB-10060, PDB-6rza: EMDB-10061, PDB-6rzb: |
| Chemicals |  ChemComp-GTP:  ChemComp-MG:  ChemComp-GDP:  ChemComp-TA1: |
| Source |
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 Keywords | MOTOR PROTEIN / filament / complex |
homo sapiens (human)
sus scrofa (pig)
mus musculus (house mouse)