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The structure of bacterial ParM filaments
- Source :
- Nature Structural & Molecular Biology. 14:921-926
- Publication Year :
- 2007
- Publisher :
- Springer Science and Business Media LLC, 2007.
-
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.
- Subjects :
- Models, Molecular
Cell division
Escherichia coli Proteins
Protein subunit
Cryoelectron Microscopy
Molecular Sequence Data
ParM
DNA replication
macromolecular substances
Protein degradation
Biology
Actins
Article
Cell biology
Protein filament
Protein Subunits
Structural Biology
Escherichia coli
Protein folding
Protein Structure, Quaternary
Molecular Biology
Actin
Subjects
Details
- ISSN :
- 15459985 and 15459993
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Nature Structural & Molecular Biology
- Accession number :
- edsair.doi.dedup.....0cde26994950ccaa457c2ada6595d0e2