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-Structure paper
Title | The structure of bacterial ParM filaments. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 14, Issue 10, Page 921-926, Year 2007 |
Publish date | Sep 16, 2007 |
Authors | Albina Orlova / Ethan C Garner / Vitold E Galkin / John Heuser / R Dyche Mullins / Edward H Egelman / |
PubMed 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 ...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. |
External links | Nat Struct Mol Biol / PubMed:17873883 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 16 Å |
Structure data | PDB-2qu4: |
Source |
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Keywords | STRUCTURAL PROTEIN / filament model / actin-like protein / helical polymer / Plasmid / Plasmid partition |