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| Title | Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 115, Issue 13, Page 3356-3361, Year 2018 |
| Publish date | Mar 27, 2018 |
 Authors | Gülsima D Usluer / Frank DiMaio / Shun Kai Yang / Jesse M Hansen / Jessica K Polka / R Dyche Mullins / Justin M Kollman /   |
| PubMed 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 ...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. |
 External links | Proc Natl Acad Sci U S A / PubMed:29440491 / PubMed Central |
| Methods | EM (helical sym.) |
| Resolution | 4.2 Å |
| Structure data | |
| Chemicals |  ChemComp-ANP: |
| Source |
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 Keywords |  CYTOSOLIC PROTEIN / actin / plasmid segregation / filament |
