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Structure paper

TitleBending forces and nucleotide state jointly regulate F-actin structure.
Journal, issue, pagesNature, Vol. 611, Issue 7935, Page 380-386, Year 2022
Publish dateOct 26, 2022
AuthorsMatthew J Reynolds / Carla Hachicho / Ayala G Carl / Rui Gong / Gregory M Alushin /
PubMed AbstractATP-hydrolysis-coupled actin polymerization is a fundamental mechanism of cellular force generation. In turn, force and actin filament (F-actin) nucleotide state regulate actin dynamics by tuning F- ...ATP-hydrolysis-coupled actin polymerization is a fundamental mechanism of cellular force generation. In turn, force and actin filament (F-actin) nucleotide state regulate actin dynamics by tuning F-actin's engagement of actin-binding proteins through mechanisms that are unclear. Here we show that the nucleotide state of actin modulates F-actin structural transitions evoked by bending forces. Cryo-electron microscopy structures of ADP-F-actin and ADP-P-F-actin with sufficient resolution to visualize bound solvent reveal intersubunit interfaces bridged by water molecules that could mediate filament lattice flexibility. Despite extensive ordered solvent differences in the nucleotide cleft, these structures feature nearly identical lattices and essentially indistinguishable protein backbone conformations that are unlikely to be discriminable by actin-binding proteins. We next introduce a machine-learning-enabled pipeline for reconstructing bent filaments, enabling us to visualize both continuous structural variability and side-chain-level detail. Bent F-actin structures reveal rearrangements at intersubunit interfaces characterized by substantial alterations of helical twist and deformations in individual protomers, transitions that are distinct in ADP-F-actin and ADP-P-F-actin. This suggests that phosphate rigidifies actin subunits to alter the bending structural landscape of F-actin. As bending forces evoke nucleotide-state dependent conformational transitions of sufficient magnitude to be detected by actin-binding proteins, we propose that actin nucleotide state can serve as a co-regulator of F-actin mechanical regulation.
External linksNature / PubMed:36289330 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.43 - 3.71 Å
Structure data

27114

8d13

EMDB-27114, PDB-8d13:
Helical ADP-F-actin
Method: EM (helical sym.) / Resolution: 2.43 Å

27115

8d14

EMDB-27115, PDB-8d14:
Helical ADP-Pi-F-actin
Method: EM (helical sym.) / Resolution: 2.51 Å

27116

8d15

EMDB-27116, PDB-8d15:
Bent ADP-F-actin
Method: EM (single particle) / Resolution: 3.61 Å

27117

8d16

EMDB-27117, PDB-8d16:
Bent ADP-Pi-F-actin
Method: EM (single particle) / Resolution: 3.71 Å

27118

8d17

EMDB-27118, PDB-8d17:
Straight ADP-F-actin 1
Method: EM (single particle) / Resolution: 3.69 Å

27119

8d18

EMDB-27119, PDB-8d18:
Straight ADP-F-actin 2
Method: EM (single particle) / Resolution: 3.66 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-PO4:
PHOSPHATE ION / Phosphate

Source
  • gallus gallus (chicken)
  • chicken (chicken)
KeywordsSTRUCTURAL PROTEIN / Cytoskeleton

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