Structural highlights
Function
PG117_VACCW Multifunctional protein required for genome uncoating and replication (PubMed:17093187, PubMed:18000036, PubMed:26912611). Major viral uncoating protein that is required for the release of the viral genome from incoming viral cores containing the viral DNA genome (PubMed:24439902). Possesses an ATPase activity that is required for hexamerization and uncoating (PubMed:24439902, PubMed:26912611).[1] [2] [3] [4] [5]
References
- ↑ Ishii K, Moss B. Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex. Virology. 2002 Nov 25;303(2):232-9. PMID:12490386 doi:10.1006/viro.2002.1721
- ↑ Boyle KA, Arps L, Traktman P. Biochemical and genetic analysis of the vaccinia virus d5 protein: Multimerization-dependent ATPase activity is required to support viral DNA replication. J Virol. 2007 Jan;81(2):844-59. PMID:17093187 doi:10.1128/JVI.02217-06
- ↑ De Silva FS, Lewis W, Berglund P, Koonin EV, Moss B. Poxvirus DNA primase. Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18724-9. PMID:18000036 doi:10.1073/pnas.0709276104
- ↑ Kilcher S, Schmidt FI, Schneider C, Kopf M, Helenius A, Mercer J. siRNA screen of early poxvirus genes identifies the AAA+ ATPase D5 as the virus genome-uncoating factor. Cell Host Microbe. 2014 Jan 15;15(1):103-12. PMID:24439902 doi:10.1016/j.chom.2013.12.008
- ↑ Hutin S, Ling WL, Round A, Effantin G, Reich S, Iseni F, Tarbouriech N, Schoehn G, Burmeister WP. Domain Organization of Vaccinia Virus Helicase-Primase D5. J Virol. 2016 Apr 14;90(9):4604-4613. PMID:26912611 doi:10.1128/JVI.00044-16
