Structural highlights
Publication Abstract from PubMedThe tegument protein U14 of human herpesvirus 6B (HHV-6B) constitutes the viral virion structure and is essential for viral growth. To define the characteristics and functions of U14, we determined the crystal structure of the N-terminal domain of HHV-6B U14 (U14-NTD) at 1.85 A resolution. U14-NTD forms an elongated helix-rich fold with a protruding beta hairpin. U14-NTD exists as a dimer exhibiting broad electrostatic interactions and a network of hydrogen bonds. This is first report of the crystal structure and dimerization of HHV-6B U14. The surface of the U14-NTD dimer reveals multiple clusters of negatively- and positively-charged residues that coincide with potential functional sites of U14. Three successive residues, L424, E425 and V426, which relate to viral growth, reside on the beta hairpin close to the dimer's two-fold axis. The hydrophobic side-chains of L424 and V426 that constitute a part of a hydrophobic patch are solvent-exposed, indicating the possibility that the beta hairpin region is a key functional site of HHV-6 U14. Structure-based sequence comparison suggests that U14-NTD corresponds to the core fold conserved among U14 homologs, human herpesvirus 7 U14, and human cytomegalovirus UL25 and UL35, although dimerization appears to be a specific feature of the U14 group. Crystal Structure of Human Herpesvirus 6B Tegument Protein U14.,Wang B, Nishimura M, Tang H, Kawabata A, Mahmoud NF, Khanlari Z, Hamada D, Tsuruta H, Mori Y PLoS Pathog. 2016 May 6;12(5):e1005594. doi: 10.1371/journal.ppat.1005594., eCollection 2016 May. PMID:27152739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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