3TXS
Crystal Structure of phage 44RR small terminase gp16
Summary for 3TXS
| Entry DOI | 10.2210/pdb3txs/pdb |
| Related | 3TXQ |
| Descriptor | Terminase DNA packaging enzyme small subunit (2 entities in total) |
| Functional Keywords | helix, small terminase, viral protein |
| Biological source | Aeromonas phage 44RR2.8t |
| Total number of polymer chains | 4 |
| Total formula weight | 43381.91 |
| Authors | Sun, S.,Xiang, Y.,Rossmann, M.G. (deposition date: 2011-09-23, release date: 2011-12-28, Last modification date: 2023-09-13) |
| Primary citation | Sun, S.,Gao, S.,Kondabagil, K.,Xiang, Y.,Rossmann, M.G.,Rao, V.B. Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages. Proc.Natl.Acad.Sci.USA, 109:817-822, 2012 Cited by PubMed Abstract: Tailed DNA bacteriophages assemble empty procapsids that are subsequently filled with the viral genome by means of a DNA packaging machine situated at a special fivefold vertex. The packaging machine consists of a "small terminase" and a "large terminase" component. One of the functions of the small terminase is to initiate packaging of the viral genome, whereas the large terminase is responsible for the ATP-powered translocation of DNA. The small terminase subunit has three domains, an N-terminal DNA-binding domain, a central oligomerization domain, and a C-terminal domain for interacting with the large terminase. Here we report structures of the central domain in two different oligomerization states for a small terminase from the T4 family of phages. In addition, we report biochemical studies that establish the function for each of the small terminase domains. On the basis of the structural and biochemical information, we propose a model for DNA packaging initiation. PubMed: 22207623DOI: 10.1073/pnas.1110224109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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