+Search query
-Structure paper
Title | Structural diversity and oligomerization of bacterial ubiquitin-like proteins. |
---|---|
Journal, issue, pages | Structure, Year 2025 |
Publish date | Apr 8, 2025 |
![]() | Minheng Gong / Qiaozhen Ye / Yajie Gu / Lydia R Chambers / Andrey A Bobkov / Neal K Arakawa / Mariusz Matyszewski / Kevin D Corbett / ![]() |
PubMed Abstract | Bacteria possess a variety of operons with homology to eukaryotic ubiquitination pathways that encode predicted E1, E2, E3, deubiquitinase, and ubiquitin-like proteins. Some of these pathways have ...Bacteria possess a variety of operons with homology to eukaryotic ubiquitination pathways that encode predicted E1, E2, E3, deubiquitinase, and ubiquitin-like proteins. Some of these pathways have recently been shown to function in anti-bacteriophage immunity, but the biological functions of others remain unknown. Here, we show that ubiquitin-like proteins in two bacterial operon families show surprising architectural diversity, possessing one to three β-grasp domains preceded by diverse N-terminal domains. We find that a large group of bacterial ubiquitin-like proteins possess three β-grasp domains and form homodimers and helical filaments mediated by conserved Ca ion binding sites. Our findings highlight a distinctive mode of self-assembly for ubiquitin-like proteins and suggest that Ca-mediated ubiquitin-like protein filament assembly and/or disassembly enables cells to sense and respond to stress conditions that alter intracellular metal ion concentration. |
![]() | ![]() ![]() |
Methods | EM (helical sym.) / EM (single particle) |
Resolution | 2.43 - 3.08 Å |
Structure data | EMDB-46576, PDB-9d59: EMDB-46577, PDB-9d5a: EMDB-46578, PDB-9d5b: |
Chemicals | ![]() ChemComp-CA: |
Source |
|
![]() | PROTEIN BINDING / filament / beta-grasp / ubiquitin |