3P9A
An atomic view of the nonameric small terminase subunit of Bacteriophage P22
Summary for 3P9A
| Entry DOI | 10.2210/pdb3p9a/pdb |
| Descriptor | DNA-packaging protein gp3 (2 entities in total) |
| Functional Keywords | terminase small subunit, dna packaging, bacteriophage p22, dna binding protein |
| Biological source | Enterobacteria phage P22 (Bacteriophage P22) |
| Total number of polymer chains | 9 |
| Total formula weight | 168075.44 |
| Authors | Bhardwaj, A.,Roy, A.,Cingolani, G. (deposition date: 2010-10-17, release date: 2012-05-09, Last modification date: 2024-02-21) |
| Primary citation | Roy, A.,Bhardwaj, A.,Datta, P.,Lander, G.C.,Cingolani, G. Small terminase couples viral DNA binding to genome-packaging ATPase activity. Structure, 20:1403-1413, 2012 Cited by PubMed Abstract: Packaging of viral genomes into empty procapsids is powered by a large DNA-packaging motor. In most viruses, this machine is composed of a large (L) and a small (S) terminase subunit complexed with a dodecamer of portal protein. Here we describe the 1.75 Å crystal structure of the bacteriophage P22 S-terminase in a nonameric conformation. The structure presents a central channel ∼23 Å in diameter, sufficiently large to accommodate hydrated B-DNA. The last 23 residues of S-terminase are essential for binding to DNA and assembly to L-terminase. Upon binding to its own DNA, S-terminase functions as a specific activator of L-terminase ATPase activity. The DNA-dependent stimulation of ATPase activity thus rationalizes the exclusive specificity of genome-packaging motors for viral DNA in the crowd of host DNA, ensuring fidelity of packaging and avoiding wasteful ATP hydrolysis. This posits a model for DNA-dependent activation of genome-packaging motors of general interest in virology. PubMed: 22771211DOI: 10.1016/j.str.2012.05.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.755 Å) |
Structure validation
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