7z8i

The barbed end complex of dynactin bound to BICDR1 and the cytoplasmic dynein tails (A2, B1, B2)

spinqualitylabelsall models 7z8i, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7z8i is a 17 chain structure with sequence from Homo sapiens, Mus musculus and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: ADP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DC1I2_HUMAN Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes. Publication Abstract from PubMed Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor(1-3). Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour(4-6). Different coiled-coil adaptors are linked to different cargos(7,8), and some share motifs known to contact sites on dynein and dynactin(4,9-13). There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos. Structure of dynein-dynactin on microtubules shows tandem adaptor binding.,Chaaban S, Carter AP Nature. 2022 Oct;610(7930):212-216. doi: 10.1038/s41586-022-05186-y. Epub 2022 , Sep 7. PMID:36071160 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dynactin Dynein 3D structures

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