Structural highlights
Publication Abstract from PubMed
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.
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.,Usluer GD, DiMaio F, Yang SK, Hansen JM, Polka JK, Mullins RD, Kollman JM Proc Natl Acad Sci U S A. 2018 Feb 13. pii: 1715836115. doi:, 10.1073/pnas.1715836115. PMID:29440491[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Usluer GD, DiMaio F, Yang SK, Hansen JM, Polka JK, Mullins RD, Kollman JM. Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain. Proc Natl Acad Sci U S A. 2018 Feb 13. pii: 1715836115. doi:, 10.1073/pnas.1715836115. PMID:29440491 doi:http://dx.doi.org/10.1073/pnas.1715836115
