Publication Abstract from PubMed
Bacterial ParM is a homolog of eukaryotic actin and is involved in moving plasmids so that they segregate properly during cell division. Using cryo-EM and three-dimensional reconstruction, we show that ParM filaments have a different structure from F-actin, with very different subunit-subunit interfaces. These interfaces result in the helical handedness of the ParM filament being opposite to that of F-actin. Like F-actin, ParM filaments have a variable twist, and we show that this involves domain-domain rotations within the ParM subunit. The present results yield new insights into polymorphisms within F-actin, as well as the evolution of polymer families.
The structure of bacterial ParM filaments.,Orlova A, Garner EC, Galkin VE, Heuser J, Mullins RD, Egelman EH Nat Struct Mol Biol. 2007 Oct;14(10):921-6. Epub 2007 Sep 16. PMID:17873883[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
