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Title

Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain

AuthorsNadal, Marta ; Mas, Philippe J.; Blanco, Alexandre G.; Arnan, Carme ; Solà, Maria ; Hart, Darren J.; Coll, Miquel
KeywordsCrystal structure
Human cytomegalovirus
DNA encapsidation
Endonuclease inhibitor
Combinatorial library
Issue Date14-Sep-2010
PublisherNational Academy of Sciences (U.S.)
CitationProceedings of the National Academy of Sciences 10(37): 16078-16083 (2010)
AbstractDuring viral replication, herpesviruses package their DNA into the procapsid by means of the terminase protein complex. In human cytomegalovirus (herpesvirus 5), the terminase is composed of subunits UL89 and UL56. UL89 cleaves the long DNA concatemers into unit-length genomes of appropriate length for encapsidation. We used ESPRIT, a high-throughput screening method, to identify a soluble purifiable fragment of UL89 from a library of 18,432 randomly truncated ul89 DNA constructs. The purified protein was crystallized and its three-dimensional structure was solved. This protein corresponds to the key nuclease domain of the terminase and shows an RNase H/integrase-like fold. We demonstrate that UL89-C has the capacity to process the DNA and that this function is dependent on Mn2+ ions, two of which are located at the active site pocket. We also show that the nuclease function can be inactivated by raltegravir, a recently approved anti-AIDS drug that targets the HIV integrase.
DescriptionEl pdf es la versión pre-print.
Publisher version (URL)http://dx.doi.org/10.1073/pnas.1007144107
URIhttp://hdl.handle.net/10261/32178
DOI10.1073/pnas.1007144107
ISSN0027-8424
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