Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix.
The bacterial actin homolog ParM has always been modeled as a polar filament, comprising two parallel helical strands, like actin itself. I present arguments here that ParM may be an apolar filament, in which the two helical strands are antiparallel.
Departments of Cell Biology, Biochemistry, and Biomedical Engineering, Duke University, Durham, NC 27710-3709, USA. h.erickson@cellbio.duke.edu
Harold P
HP
Erickson
D008841:Actin Cytoskeleton / Q000737:chemistry*; D000199:Actins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary
D000199:Actins; D029968:Escherichia coli Proteins; C471255:ParM protein, E coli