| Literature DB >> 15063737 |
Christos G W Savva1, Andreas Holzenburg, Elke Bogner.
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.Entities:
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Year: 2004 PMID: 15063737 DOI: 10.1016/S0014-5793(04)00283-2
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124