Structural highlights
Function
VINT_SSV1 This protein may encode a site-specific integrase, which is necessary for integration of the phage by site-specific recombination into a tRNA gene of the host chromosome. Essential for virus infection.[1] [2]
Publication Abstract from PubMed
The first structure of a catalytic domain from a hyperthermophilic archaeal viral integrase reveals a minimal fold similar to that of bacterial HP1 integrase and defines structural elements conserved across three domains of life. However, structural superposition on bacterial Holliday junction complexes and similarities in the C-terminal tail with that of eukaryotic Flp suggest that the catalytic tyrosine and an additional active-site lysine are delivered to neighboring subunits in trans. An intramolecular disulfide bond contributes significant thermostability in vitro.
The Structure of an Archaeal Viral Integrase Reveals an Evolutionarily Conserved Catalytic Core yet Supports a Mechanism of DNA Cleavage in trans.,Eilers BJ, Young MJ, Lawrence CM J Virol. 2012 Aug;86(15):8309-13. Epub 2012 May 16. PMID:22593158[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stedman KM, Schleper C, Rumpf E, Zillig W. Genetic requirements for the function of the archaeal virus SSV1 in Sulfolobus solfataricus: construction and testing of viral shuttle vectors. Genetics. 1999 Aug;152(4):1397-405. PMID:10430570
- ↑ Zhan Z, Ouyang S, Liang W, Zhang Z, Liu ZJ, Huang L. Structural and functional characterization of the C-terminal catalytic domain of SSV1 integrase. Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):659-70. doi:, 10.1107/S0907444912007202. Epub 2012 May 17. PMID:22683788 doi:http://dx.doi.org/10.1107/S0907444912007202
- ↑ Eilers BJ, Young MJ, Lawrence CM. The Structure of an Archaeal Viral Integrase Reveals an Evolutionarily Conserved Catalytic Core yet Supports a Mechanism of DNA Cleavage in trans. J Virol. 2012 Aug;86(15):8309-13. Epub 2012 May 16. PMID:22593158 doi:10.1128/JVI.00547-12
