6djo

Cryo-EM structure of ADP-actin filaments

spinqualitylabelsall models 6djo, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6djo is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG NonStd Res: HIC Related: 6djn, 6djm Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACTS_CHICK] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMed We used cryo-electron microscopy (cryo-EM) to reconstruct actin filaments with bound AMPPNP (beta,gamma-imidoadenosine 5'-triphosphate, an ATP analog, resolution 3.1 A), ADP-Pi (ADP with inorganic phosphate, resolution 3.1 A), or ADP (resolution 3.6 A). Subunits in the three filaments have similar backbone conformations, so assembly rather than ATP hydrolysis or phosphate dissociation is responsible for their flattened conformation in filaments. Polymerization increases the rate of ATP hydrolysis by changing the positions of the side chains of Q137 and H161 in the active site. Flattening during assembly also promotes interactions along both the long-pitch and short-pitch helices. In particular, conformational changes in subdomain 3 open up multiple favorable interactions with the DNase-I binding loop in subdomain 2 of the adjacent subunit. Subunits at the barbed end of the filament are likely to be in this favorable conformation, while monomers are not. This difference explains why filaments grow faster at the barbed end than the pointed end. When phosphate dissociates from ADP-Pi-actin through a backdoor channel, the conformation of the C terminus changes so it distorts the DNase binding loop, which allows cofilin binding, and a network of interactions among S14, H73, G74, N111, R177, and G158 rearranges to open the phosphate release site. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.,Chou SZ, Pollard TD Proc Natl Acad Sci U S A. 2019 Feb 13. pii: 1807028115. doi:, 10.1073/pnas.1807028115. PMID:30760599 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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