Insights into the structure of human cytomegalovirus large terminase subunit pUL56 |
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Authors: | Savva Christos G W Holzenburg Andreas Bogner Elke |
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Institution: | Microscopy and Imaging Center, Department of Biology, Texas A and M University, College Station, TX 77843-2257, USA. |
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Abstract: | Terminases are a class of proteins which catalyze the generation of unit-length genomes during DNA packaging. These essential proteins are conserved throughout the herpesviruses and many double-stranded DNA bacteriophages. We have determined the structure of the large terminase subunit pUL56 of human cytomegalovirus, a highly pathogenic virus, to 2.6 nm resolution. Image analysis of purified pUL56 suggests that the molecule exists as a dimer formed by the association of two ring-like structures positioned on top of each other and connected by a pronounced density on one side. The 3D reconstruction of pUL56 provides first structural insights into the active protein. |
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