Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1.

ABSTRACT: 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

SUBMITTER: Bowman BR 

PROVIDER: S-EPMC1395411 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature