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Structure paper

TitleStructural basis of actin filament assembly and aging.
Journal, issue, pagesNature, Vol. 611, Issue 7935, Page 374-379, Year 2022
Publish dateOct 26, 2022
AuthorsWout Oosterheert / Björn U Klink / Alexander Belyy / Sabrina Pospich / Stefan Raunser /
PubMed AbstractThe 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.
External linksNature / PubMed:36289337 / PubMed Central
MethodsEM (single particle)
Resolution2.15 - 2.24 Å
Structure data

15104

8a2r

EMDB-15104, PDB-8a2r:
Cryo-EM structure of F-actin in the Mg2+-ADP-BeF3- nucleotide state.
Method: EM (single particle) / Resolution: 2.17 Å

15105

8a2s

EMDB-15105, PDB-8a2s:
Cryo-EM structure of F-actin in the Mg2+-ADP-Pi nucleotide state.
Method: EM (single particle) / Resolution: 2.22 Å

15106

8a2t

EMDB-15106, PDB-8a2t:
Cryo-EM structure of F-actin in the Mg2+-ADP nucleotide state.
Method: EM (single particle) / Resolution: 2.24 Å

15107

8a2u

EMDB-15107, PDB-8a2u:
Cryo-EM structure of F-actin in the Ca2+-ADP-BeF3- nucleotide state.
Method: EM (single particle) / Resolution: 2.21 Å

15108

8a2y

EMDB-15108, PDB-8a2y:
Cryo-EM structure of F-actin in the Ca2+-ADP-Pi nucleotide state.
Method: EM (single particle) / Resolution: 2.15 Å

15109

8a2z

EMDB-15109, PDB-8a2z:
Cryo-EM structure of F-actin in the Ca2+-ADP nucleotide state.
Method: EM (single particle) / Resolution: 2.15 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-CA:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
  • rabbit (rabbit)
KeywordsSTRUCTURAL PROTEIN / actin / cytoskeleton / filament / nucleotide state

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