8E9B
Cryo-EM structure of S. pombe Arp2/3 complex in the branch junction
Summary for 8E9B
| Entry DOI | 10.2210/pdb8e9b/pdb |
| EMDB information | 27962 |
| Descriptor | Actin-related protein 3, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (11 entities in total) |
| Functional Keywords | arp2-3 complex, branch juction, polymerization, structural protein |
| Biological source | Schizosaccharomyces pombe (fission yeast) More |
| Total number of polymer chains | 15 |
| Total formula weight | 566408.19 |
| Authors | |
| Primary citation | Chou, S.Z.,Chatterjee, M.,Pollard, T.D. Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction. Proc.Natl.Acad.Sci.USA, 119:e2206722119-e2206722119, 2022 Cited by PubMed Abstract: We reconstructed the structure of actin filament branch junctions formed by fission yeast Arp2/3 complex at 3.5 Å resolution from images collected by electron cryo-microscopy. During specimen preparation, all of the actin subunits and Arp3 hydrolyzed their bound adenosine triphosphate (ATP) and dissociated the γ-phosphate, but Arp2 retained the γ-phosphate. Binding tightly to the side of the mother filament and nucleating the daughter filament growing as a branch requires Arp2/3 complex to undergo a dramatic conformational change where two blocks of structure rotate relative to each other about 25° to align Arp2 and Arp3 as the first two subunits in the branch. During branch formation, Arp2/3 complex acquires more than 8,000 Å of new buried surface, accounting for the stability of the branch. Inactive Arp2/3 complex binds only transiently to the side of an actin filament, because its conformation allows only a subset of the interactions found in the branch junction. PubMed: 36442092DOI: 10.1073/pnas.2206722119 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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