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TitleCryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 13, Page 3356-3361, Year 2018
Publish dateMar 27, 2018
AuthorsGülsima D Usluer / Frank DiMaio / Shun Kai Yang / Jesse M Hansen / Jessica K Polka / R Dyche Mullins / Justin M Kollman /
PubMed AbstractBacterial 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 linksProc Natl Acad Sci U S A / PubMed:29440491 / PubMed Central
MethodsEM (helical sym.)
Resolution4.2 Å
Structure data

7134

6bqw

EMDB-7134, PDB-6bqw:
AlfA Filament bound to AMPPNP
Method: EM (helical sym.) / Resolution: 4.2 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • bacillus subtilis (bacteria)
KeywordsCYTOSOLIC PROTEIN / actin / plasmid segregation / filament

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