2O0H
T4 gp17 ATPase domain mutant complexed with ATP
Summary for 2O0H
| Entry DOI | 10.2210/pdb2o0h/pdb |
| Related | 2O0J 2O0K |
| Descriptor | DNA packaging protein Gp17, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | nucleotide-binding fold, hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 44732.28 |
| Authors | Sun, S.,Rossmann, M.G. (deposition date: 2006-11-27, release date: 2007-04-03, Last modification date: 2023-12-27) |
| Primary citation | Sun, S.,Kondabagil, K.,Gentz, P.M.,Rossmann, M.G.,Rao, V.B. The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids MOL.CELL, 25:943-949, 2007 Cited by PubMed Abstract: Packaging the viral genome into empty procapsids, an essential event in the life cycle of tailed bacteriophages and some eukaryotic viruses, is a process that shares features with chromosome assembly. Most viral procapsids possess a special vertex containing a dodecameric portal protein that is used for entry and exit of the viral genome. The portal and an ATPase are parts of the genome-packaging machine. The ATPase is required to provide energy for translocation and compaction of the negative charges on the genomic DNA. Here we report the atomic structure of the ATPase component in a phage DNA-packaging machine. The bacteriophage T4 ATPase has the greatest similarity to monomeric helicases, suggesting that the genome is translocated by an inchworm mechanism. The similarity of the packaging machines in the double-stranded DNA (dsDNA) bacteriophage T4 and dsRNA bacteriophage varphi12 is consistent with the evolution of many virions from a common ancestor. PubMed: 17386269DOI: 10.1016/j.molcel.2007.02.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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