5afu

Cryo-EM structure of dynein tail-dynactin-BICD2N complexCryo-EM structure of dynein tail-dynactin-BICD2N complex

5afu, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Structural highlights 5afu is a 19 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.5Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0J9X2A1_PIG Publication Abstract from PubMed Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of beta-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the alpha-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components. The structure of the dynactin complex and its interaction with dynein.,Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP Science. 2015 Mar 27;347(6229):1441-6. doi: 10.1126/science.aaa4080. Epub 2015, Feb 12. PMID:25814576 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dynactin Dynein 3D structures F-actin capping protein