+Search query
-Structure paper
Title | Filament structure of bacterial tubulin homologue TubZ. |
---|---|
Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 107, Issue 46, Page 19766-19771, Year 2010 |
Publish date | Nov 16, 2010 |
Authors | Christopher H S Aylett / Qing Wang / Katharine A Michie / Linda A Amos / Jan Löwe / |
PubMed Abstract | Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a ...Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a polymerizing cytomotive filament. Together these components drive newly replicated plasmids to opposite ends of the dividing cell. The Bacillus thuringiensis plasmid pBToxis relies on a filament of the tubulin/FtsZ-like protein TubZ for its segregation. By combining crystallography and electron microscopy, we have determined the structure of this filament. We explain how GTP hydrolysis weakens the subunit-subunit contact and also shed light on the partitioning of the plasmid-adaptor complex. The double helical superstructure of TubZ filaments is unusual for tubulin-like proteins. Filaments of ParM, the actin-like partitioning protein, are also double helical. We suggest that convergent evolution shapes these different types of cytomotive filaments toward a general mechanism for plasmid separation. |
External links | Proc Natl Acad Sci U S A / PubMed:20974911 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 3 - 35.0 Å |
Structure data | EMDB-1757: EMDB-1758: EMDB-1759: EMDB-1760: PDB-2xka: PDB-2xkb: |
Chemicals | ChemComp-GSP: ChemComp-MG: ChemComp-GDP: |
Source |
|
Keywords | STRUCTURAL PROTEIN / MOTOR PROTEIN / CYTOSKELETON / CYTOMOTIVE / DNA SEGREGATION / MICROTUBULE / PBTOXIS / PBT156 / REPX / TUBR |