4xcq

Clostridium botulinum phage c-st TubZ (C-terminal tail truncated protein)

spinqualitylabelsall models 4xcq, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xcq is a 1 chain structure with sequence from Clostridium phage c-st. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.39Å Ligands: GDP, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TUBZ_CBCP A tubulin-like, filament forming GTPase; the motor component of the type III partition system presumably used to ensure correct segregation of this bacteriophage. In the presence of Mg(2+) and GTP (or GTP-gamma-S) assembles into filaments which upon polymerization are almost exclusively bound to GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed. Unlike its plasmid homolog in B.thuringiensis (AC Q8KNP3) GTP-gamma-S does not alter filament formation (PubMed:22538818, PubMed:28230082). When forced to assemble with GDP instead of GTP it makes much stiffer, thicker filaments (PubMed:28230082). The filaments bind a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments (PubMed:22538818). Highly dynamic filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling phage DNA within the cell (By similarity).[UniProtKB:Q8KNP3]

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