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Insights into the structure of human cytomegalovirus large terminase subunit pUL56
Author(s) -
Savva Christos G.W,
Holzenburg Andreas,
Bogner Elke
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00283-2
Subject(s) - protein subunit , dimer , dna , human cytomegalovirus , capsid , biology , cytomegalovirus , genome , resolution (logic) , virology , virus , chemistry , herpesviridae , genetics , gene , organic chemistry , artificial intelligence , viral disease , computer science
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.