3RB8
Structure of the phage tubulin PhuZ(SeMet)-GDP
Summary for 3RB8
| Entry DOI | 10.2210/pdb3rb8/pdb |
| Related | 3R4V |
| Descriptor | Putative uncharacterized protein, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | tubulin, unknown function |
| Biological source | Pseudomonas phage 201phi2-1 |
| Total number of polymer chains | 1 |
| Total formula weight | 35458.12 |
| Authors | Agard, D.A.,Pogliano, J.,Kraemer, J.A.,Erb, M.L.,Waddling, C.A.,Montabana, E.A.,Wang, H.,Nguyen, K.,Pham, S. (deposition date: 2011-03-28, release date: 2012-07-04, Last modification date: 2024-11-20) |
| Primary citation | Kraemer, J.A.,Erb, M.L.,Waddling, C.A.,Montabana, E.A.,Zehr, E.A.,Wang, H.,Nguyen, K.,Pham, D.S.,Agard, D.A.,Pogliano, J. A phage tubulin assembles dynamic filaments by an atypical mechanism to center viral DNA within the host cell. Cell(Cambridge,Mass.), 149:1488-1499, 2012 Cited by PubMed Abstract: Tubulins are essential for the reproduction of many eukaryotic viruses, but historically, bacteriophage were assumed not to require a cytoskeleton. Here, we identify a tubulin-like protein, PhuZ, from bacteriophage 201φ2-1 and show that it forms filaments in vivo and in vitro. The PhuZ structure has a conserved tubulin fold, with an unusual, extended C terminus that we demonstrate to be critical for polymerization in vitro and in vivo. Longitudinal packing in the crystal lattice mimics packing observed by EM of in-vitro-formed filaments, indicating how interactions between the C terminus and the following monomer drive polymerization. PhuZ forms a filamentous array that is required for positioning phage DNA within the bacterial cell. Correct positioning to the cell center and optimal phage reproduction only occur when the PhuZ filament is dynamic. Thus, we show that PhuZ assembles a spindle-like array that functions analogously to the microtubule-based spindles of eukaryotes. PubMed: 22726436DOI: 10.1016/j.cell.2012.04.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report






