8ZRA

GerQ filaments from Bacillus amyloiquefaciens

Summary for 8ZRA

• Entry DOI: 10.2210/pdb8zra/pdb
• EMDB information: 60394
• Descriptor: Spore coat protein GerQ (1 entity in total)
• Functional Keywords: endospores, gerq, spore coat protein, protein fibril
• Biological source: Bacillus amyloliquefaciens (Bacillus velezensis)
• Total number of polymer chains: 18
• Total formula weight: 366462.74

Authors

Kreutzberger, M.,Egelman, E.,Cao, Q. (deposition date: 2024-06-04, release date: 2024-10-02)

Primary citation

Cheng, Y.,Kreutzberger, M.A.B.,Han, J.,Egelman, E.H.,Cao, Q.
Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM.
Nat Commun, 15:8091-8091, 2024

PubMed Abstract: 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-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.

PubMed: 39284816
DOI: 10.1038/s41467-024-52422-2

Experimental method

ELECTRON MICROSCOPY (3.32 Å)