Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate and a four-stranded filament upon GTP hydrolysis.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 111, Issue 9, Page 3407-3412, Year 2014
Publish date	Mar 4, 2014
Authors	Elizabeth A Montabana / David A Agard /
PubMed Abstract	Cytoskeletal filaments form diverse superstructures that are highly adapted for specific functions. The recently discovered TubZ subfamily of tubulins is involved in type III plasmid partitioning ...Cytoskeletal filaments form diverse superstructures that are highly adapted for specific functions. The recently discovered TubZ subfamily of tubulins is involved in type III plasmid partitioning systems, facilitating faithful segregation of low copy-number plasmids during bacterial cell division. One such protein, TubZ-Bt, is found on the large pBtoxis plasmid in Bacillus thuringiensis, and interacts via its extended C terminus with a DNA adaptor protein TubR. Here, we use cryo-electron microscopy to determine the structure of TubZ-Bt filaments and light scattering to explore their mechanism of polymerization. Surprisingly, we find that the helical filament architecture is remarkably sensitive to nucleotide state, changing from two-stranded to four-stranded depending on the ability of TubZ-Bt to hydrolyze GTP. We present pseudoatomic models of both the two- and four-protofilament forms based on cryo-electron microscopy reconstructions (10.8 Å and 6.9 Å, respectively) of filaments formed under different nucleotide states. These data lead to a model in which the two-stranded filament is a necessary intermediate along the pathway to formation of the four-stranded filament. Such nucleotide-directed structural polymorphism is to our knowledge an unprecedented mechanism for the formation of polar filaments.
External links	Proc Natl Acad Sci U S A / PubMed:24550513 / PubMed Central
Methods	EM (helical sym.)
Resolution	6.8 - 10.8 Å
Structure data	5762 3j4s EMDB-5762: Electron cryo-microscopy of four-stranded TubZ from B. thuringiensis PDB-3j4s: Helical Model of TubZ-Bt four-stranded filament Method: EM (helical sym.) / Resolution: 6.9 Å 5763 3j4t EMDB-5763: Electron cryo-microscopy of two-stranded TubZ filament from B. thuringiensis PDB-3j4t: Helical model of TubZ-Bt two-stranded filament Method: EM (helical sym.) / Resolution: 10.8 Å
Chemicals	ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate
Source	bacillus thuringiensis (bacteria)
Keywords	STRUCTURAL PROTEIN / FtsZ-like / Tubulin-like / GTPase / TubZ / plasmid segregation