Structural highlights
Function
[UL25_HHV11] Plays a role at the late stage in the encapsidation of viral DNA, assuring correct genome cleavage and presumably stabilizing capsids that contain full-lengtht viral genomes. Located on the external vertices of the T=16 icosahedric capsid, may bind together the tegument and the capsid through interaction with large tegument protein UL36. Could mediate, via binding to host nucleoporin NUC214, the capsid docking to the nuclear pore allowing entry of the viral genome into the nucleus.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Herpesviruses replicate their double stranded DNA genomes as high-molecular-weight concatemers which are subsequently cleaved into unit-length genomes by a complex mechanism that is tightly coupled to DNA insertion into a preformed capsid structure, the procapsid. The herpes simplex virus type 1 UL25 protein is incorporated into the capsid during DNA packaging, and previous studies of a null mutant have demonstrated that its function is essential at the late stages of the head-filling process, either to allow packaging to proceed to completion or for retention of the viral genome within the capsid. We have expressed and purified an N-terminally truncated form of the 580-residue UL25 protein and have determined the crystallographic structure of the region corresponding to amino acids 134 to 580 at 2.1-Angstroms resolution. This structure, the first for any herpesvirus protein involved in processing and packaging of viral DNA, reveals a novel fold, a distinctive electrostatic distribution, and a unique "flexible" architecture in which numerous flexible loops emanate from a stable core. Evolutionary trace analysis of UL25 and its homologues in other herpesviruses was used to locate potentially important amino acids on the surface of the protein, leading to the identification of four putative docking regions for protein partners.
Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1.,Bowman BR, Welschhans RL, Jayaram H, Stow ND, Preston VG, Quiocho FA J Virol. 2006 Mar;80(5):2309-17. PMID:16474137[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Preston VG, Murray J, Preston CM, McDougall IM, Stow ND. The UL25 gene product of herpes simplex virus type 1 is involved in uncoating of the viral genome. J Virol. 2008 Jul;82(13):6654-66. doi: 10.1128/JVI.00257-08. Epub 2008 Apr 30. PMID:18448531 doi:http://dx.doi.org/10.1128/JVI.00257-08
- ↑ Cockrell SK, Sanchez ME, Erazo A, Homa FL. Role of the UL25 protein in herpes simplex virus DNA encapsidation. J Virol. 2009 Jan;83(1):47-57. doi: 10.1128/JVI.01889-08. Epub 2008 Oct 22. PMID:18945788 doi:http://dx.doi.org/10.1128/JVI.01889-08
- ↑ Bowman BR, Welschhans RL, Jayaram H, Stow ND, Preston VG, Quiocho FA. Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1. J Virol. 2006 Mar;80(5):2309-17. PMID:16474137 doi:80/5/2309
