6RZB

Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules

Summary for 6RZB

• Entry DOI: 10.2210/pdb6rzb/pdb
• EMDB information: 10061
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, MKIAA0325 protein, ... (7 entities in total)
• Functional Keywords: filament, complex, motor protein
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 3
• Total formula weight: 115243.08

Authors

Lacey, S.E.,He, S.,Scheres, S.H.W.,Carter, A.P. (deposition date: 2019-06-13, release date: 2019-07-10, Last modification date: 2024-05-22)

Primary citation

Lacey, S.E.,He, S.,Scheres, S.H.,Carter, A.P.
Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.
Elife, 8:-, 2019

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 (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.

PubMed: 31264960
DOI: 10.7554/eLife.47145

Experimental method

ELECTRON MICROSCOPY (4.1 Å)