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TitleCryo-EM reconstruction of yeast ADP-actin filament at 2.5 Å resolution. A comparison with vertebrate F-actin.
Journal, issue, pagesStructure, Vol. 33, Issue 3, Page 435-442.e3, Year 2025
Publish dateMar 6, 2025
AuthorsSarah R Stevenson / Svetomir B Tzokov / Indrajit Lahiri / Kathryn R Ayscough / Per A Bullough /
PubMed AbstractThe core component of the actin cytoskeleton is the globular protein G-actin, which reversibly polymerizes into filaments (F-actin). Budding yeast possesses a single actin that shares 87%-89% ...The core component of the actin cytoskeleton is the globular protein G-actin, which reversibly polymerizes into filaments (F-actin). Budding yeast possesses a single actin that shares 87%-89% sequence identity with vertebrate actin isoforms. Previous structural studies indicate very close overlap of main-chain backbones. Intriguingly, however, substitution of yeast ACT1 with vertebrate β-cytoplasmic actin severely disrupts cell function and the substitution with a skeletal muscle isoform is lethal. Here we report a 2.5 Å structure of budding yeast F-actin. Previously unresolved side-chain information allows us to highlight four main differences in the comparison of yeast and vertebrate ADP F-actins: a more open nucleotide binding pocket; a more solvent exposed C-terminus; a rearrangement of inter-subunit binding interactions in the vicinity of the D loop and changes in the hydrogen bonding network in the vicinity of histidine 73 (yeast actin) and methyl-histidine 73 (vertebrate actin).
External linksStructure / PubMed:39798573
MethodsEM (helical sym.)
Resolution2.5 Å
Structure data

51491

9go5

EMDB-51491, PDB-9go5:
CryoEM Reconstruction of Yeast ADP-Actin Filament at 2.5 A resolution.
Method: EM (helical sym.) / Resolution: 2.5 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN FIBRIL / Fibre / polymer / helical protein / motility

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