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

The structure of bacterial ParM filaments.

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1
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-0733, USA.

Abstract

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
PMCID:
PMC3541950
DOI:
10.1038/nsmb1300
[Indexed for MEDLINE]
Free PMC Article
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