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Yorodumi- PDB-8a2s: Cryo-EM structure of F-actin in the Mg2+-ADP-Pi nucleotide state. -
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-Basic information
Entry | Database: PDB / ID: 8a2s | |||||||||||||||
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Title | Cryo-EM structure of F-actin in the Mg2+-ADP-Pi nucleotide state. | |||||||||||||||
Components | Actin, alpha skeletal muscle | |||||||||||||||
Keywords | STRUCTURAL PROTEIN / actin / cytoskeleton / filament / nucleotide state | |||||||||||||||
Function / homology | Function and homology information cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament ...cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / cell body / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / ATP binding / identical protein binding / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Oryctolagus cuniculus (rabbit) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.22 Å | |||||||||||||||
Authors | Oosterheert, W. / Klink, B.U. / Belyy, A. / Pospich, S. / Raunser, S. | |||||||||||||||
Funding support | European Union, Germany, 4items
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Citation | Journal: Nature / Year: 2022 Title: Structural basis of actin filament assembly and aging. Authors: Wout Oosterheert / Björn U Klink / Alexander Belyy / Sabrina Pospich / Stefan Raunser / Abstract: The dynamic turnover of actin filaments (F-actin) controls cellular motility in eukaryotes and is coupled to changes in the F-actin nucleotide state. It remains unclear how F-actin hydrolyses ATP and ...The dynamic turnover of actin filaments (F-actin) controls cellular motility in eukaryotes and is coupled to changes in the F-actin nucleotide state. It remains unclear how F-actin hydrolyses ATP and subsequently undergoes subtle conformational rearrangements that ultimately lead to filament depolymerization by actin-binding proteins. Here we present cryo-electron microscopy structures of F-actin in all nucleotide states, polymerized in the presence of Mg or Ca at approximately 2.2 Å resolution. The structures show that actin polymerization induces the relocation of water molecules in the nucleotide-binding pocket, activating one of them for the nucleophilic attack of ATP. Unexpectedly, the back door for the subsequent release of inorganic phosphate (P) is closed in all structures, indicating that P release occurs transiently. The small changes in the nucleotide-binding pocket after ATP hydrolysis and P release are sensed by a key amino acid, amplified and transmitted to the filament periphery. Furthermore, differences in the positions of water molecules in the nucleotide-binding pocket explain why Ca-actin shows slower polymerization rates than Mg-actin. Our work elucidates the solvent-driven rearrangements that govern actin filament assembly and aging and lays the foundation for the rational design of drugs and small molecules for imaging and therapeutic applications. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 8a2s.cif.gz | 399.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8a2s.ent.gz | 276.5 KB | Display | PDB format |
PDBx/mmJSON format | 8a2s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8a2s_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 8a2s_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 8a2s_validation.xml.gz | 64.9 KB | Display | |
Data in CIF | 8a2s_validation.cif.gz | 98.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a2/8a2s ftp://data.pdbj.org/pub/pdb/validation_reports/a2/8a2s | HTTPS FTP |
-Related structure data
Related structure data | 15105MC 8a2rC 8a2tC 8a2uC 8a2yC 8a2zC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
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Deposited unit |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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