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    Nat Struct Mol Biol. 2007 Oct;14(10):921-6. Epub 2007 Sep 16.

    The structure of bacterial ParM filaments.

    Orlova A, Garner EC, Galkin VE, Heuser J, Mullins RD, Egelman EH.

    Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-0733, USA.

    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.

    PMID: 17873883 [PubMed - indexed for MEDLINE]

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