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TitleA family of bacterial actin homologs forms a three-stranded tubular structure.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 11, Page e2500913122, Year 2025
Publish dateMar 18, 2025
AuthorsJulien R C Bergeron / Shamar L M Lale-Farjat / Hanna M Lewicka / Chloe Parry / Justin M Kollman /
PubMed AbstractThe cytoskeleton is crucial for cell organization and movement. In Eukaryotes, it largely consists of the protein actin, that forms a double-stranded linear filamentous structure in the presence of ...The cytoskeleton is crucial for cell organization and movement. In Eukaryotes, it largely consists of the protein actin, that forms a double-stranded linear filamentous structure in the presence of ATP and disassemble upon ATP hydrolysis. Bacteria also possess actin homologs, that drive fundamental cellular processes, including cell division, shape maintenance, and DNA segregation. Like eukaryotic actin, bacterial actins assemble into dynamic polymers upon ATP binding, however variation in interactions between strands gives rise to striking diversity of filament architectures. Here, we report a family of bacterial actins of unknown function, conserved among the phylum, which assembles into a unique tubular structure in the presence of ATP. A cryo-EM structure of the filaments reveals that it consists of three strands, unlike other described bacterial actin structures. This architecture provides further insights into the organization of actin-like filaments and has implications for understanding the diversity and evolution of the bacterial cytoskeleton.
External linksProc Natl Acad Sci U S A / PubMed:40073056 / PubMed Central
MethodsEM (helical sym.)
Resolution3.1 Å
Structure data

EMDB-18852, PDB-8r2n:
Structure of the BeeR filament
Method: EM (helical sym.) / Resolution: 3.1 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • opitutus terrae (bacteria)
KeywordsSTRUCTURAL PROTEIN / Bacterial cytoskeleton / actin homologue

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