5OOE
Cryo-EM structure of F-actin in complex with AppNHp (AMPPNP)
Summary for 5OOE
| Entry DOI | 10.2210/pdb5ooe/pdb |
| Related | 5ONV 5OOC 5OOD 5OOE 5OOF |
| EMDB information | 3835 3836 3837 3838 3838 3839 |
| Descriptor | Actin, alpha skeletal muscle, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | cytoskeleton, nucleotide states, filament stability, cell migration, structural protein |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 5 |
| Total formula weight | 212030.67 |
| Authors | Merino, F.,Pospich, S.,Funk, J.,Kuellmer, F.,Arndt, H.-D.,Bieling, P.,Raunser, S. (deposition date: 2017-08-07, release date: 2018-06-13) |
| Primary citation | Merino, F.,Pospich, S.,Funk, J.,Wagner, T.,Kullmer, F.,Arndt, H.D.,Bieling, P.,Raunser, S. Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. Nat. Struct. Mol. Biol., 25:528-537, 2018 Cited by PubMed Abstract: The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (P) release results in a gradient of ATP, ADP-P and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the γ-phosphate. Nucleotide hydrolysis and P release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction. PubMed: 29867215DOI: 10.1038/s41594-018-0074-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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