3J5V

PhuZ201 filament

Summary for 3J5V

• Entry DOI: 10.2210/pdb3j5v/pdb
• Related: 3R4V
• EMDB information: 5783
• Descriptor: PhuZ201 subunit, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: phuz, tubulin, ftsz, filament, bacteriophage, cytoskeleton, bacteriophage centering function, viral protein
• Biological source: Pseudomonas phage 201phi2-1
• Total number of polymer chains: 1
• Total formula weight: 35567.51

Authors

Zehr, E.A. (deposition date: 2013-11-20, release date: 2014-03-26, Last modification date: 2024-02-21)

Primary citation

Zehr, E.A.,Kraemer, J.K.,Erb, M.L.,Coker, J.K.C.,Montabana, E.A.,Pogliano, J.,Agard, D.A.
The Structure and Assembly Mechanism of a Novel Three-Stranded Tubulin Filament that Centers Phage DNA
Structure, 22:1-10, 2014

PubMed Abstract: Tubulins are a universally conserved protein superfamily that carry out diverse biological roles by assembling filaments with very different architectures. The underlying basis of this structural diversity is poorly understood. Here, we determine a 7.1 Å cryo-electron microscopy reconstruction of the bacteriophage-encoded PhuZ filament and provide molecular-level insight into its cooperative assembly mechanism. The PhuZ family of tubulins is required to actively center the phage within infected host cells, facilitating efficient phage replication. Our reconstruction and derived model reveal the first example of a three-stranded tubulin filament. We show that the elongated C-terminal tail simultaneously stabilizes both longitudinal and lateral interactions, which in turn define filament architecture. Identified interaction surfaces are conserved within the PhuZ family, and their mutagenesis compromises polymerization in vitro and in vivo. Combining kinetic modeling of PhuZ filament assembly and structural data, we suggest a common filament structure and assembly mechanism for the PhuZ family of tubulins.

PubMed: 24631461
DOI: 10.1016/j.str.2014.02.006

Experimental method

ELECTRON MICROSCOPY (7.1 Å)