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Publication Abstract from PubMed

Protein filaments are ubiquitous in nature and have diverse biological functions. Cryo-electron microscopy (cryo-EM) enables the determination of atomic structures, even from native samples, and is capable of identifying previously unknown filament species through high-resolution cryo-EM maps. In this study, we determine the structure of an unreported filament species from a cryo-EM dataset collected from Bacillus amyloiquefaciens biofilms. These filaments are composed of GerQ, a spore coat protein known to be involved in Bacillus spore germination. GerQ assembles into a structurally stable architecture consisting of rings containing nine subunits, which stacks to form filaments. Molecular dockings and model predictions suggest that this nine-subunit structure is suitable for binding CwlJ, a protein recruited by GerQ and essential for Ca(2+)-DPA induced spore germination. While the assembly state of GerQ within the spores and the direct interaction between GerQ and CwlJ have yet to be validated through further experiments, our findings provide valuable insights into the self-assembly of GerQ and enhance our understanding of its role in spore germination.

Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM.,Cheng Y, Kreutzberger MAB, Han J, Egelman EH, Cao Q Nat Commun. 2024 Sep 16;15(1):8091. doi: 10.1038/s41467-024-52422-2. PMID:39284816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.