| Literature DB >> 17873883 |
Albina Orlova1, Ethan C Garner, Vitold E Galkin, John Heuser, R Dyche Mullins, Edward H Egelman.
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.Mesh:
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Year: 2007 PMID: 17873883 PMCID: PMC3541950 DOI: 10.1038/nsmb1300
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369