ArticleProceedings of the National Academy of Sciences of the United States of America2018
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Actin network evolution as a key driver of eukaryotic diversification.Journal of cell science · 2024Review
- Archaeal actins and the origin of a multi-functional cytoskeleton.Journal of bacteriology · 2024Review
- The evolution of archaeal flagellar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The structure of a 15-stranded actin-like filament from Clostridium botulinum.Nature communications · 2019Article
- Plasmid Localization and Partition inEcoSal Plus · 2019Review
- The complex simplicity of the bacterial cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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7 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial actins are an evolutionarily diverse family of ATP-dependent filaments built from protomers with a conserved structural fold. Actin-based segregation systems are encoded on many bacterial plasmids and function to partition plasmids into daughter cells. The bacterial actin AlfA segregates plasmids by a mechanism distinct from other partition systems, dependent on its unique dynamic properties. Here, we report the near-atomic resolution electron cryo-microscopy structure of the AlfA filament, which reveals a strikingly divergent filament architecture resulting from the loss of a subdomain conserved in all other actins and a mode of ATP binding. Its unusual assembly interfaces and nucleotide interactions provide insight into AlfA dynamics, and expand the range of evolutionary variation accessible to actin quaternary structure.
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