5B1Q

Human herpesvirus 6B tegument protein U14

Summary for 5B1Q

• Entry DOI: 10.2210/pdb5b1q/pdb
• Descriptor: U14 protein, GLYCEROL (3 entities in total)
• Functional Keywords: herpesvirus, tegument, homodimer, viral protein
• Biological source: Human herpesvirus 6B (strain HST) (HHV-6 variant B)
• Total number of polymer chains: 2
• Total formula weight: 105522.85

Authors

Wang, B.,Nishimura, M.,Tang, H.,Kawabata, A.,Mahmoud, N.F.,Khanlari, Z.,Hamada, D.,Tsuruta, H.,Mori, Y. (deposition date: 2015-12-11, release date: 2016-04-20, Last modification date: 2024-03-20)

Primary citation

Wang, B.,Nishimura, M.,Tang, H.,Kawabata, A.,Mahmoud, N.F.,Khanlari, Z.,Hamada, D.,Tsuruta, H.,Mori, Y.
Crystal Structure of Human Herpesvirus 6B Tegument Protein U14.
Plos Pathog., 12:e1005594-e1005594, 2016

PubMed Abstract: The 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 Å resolution. U14-NTD forms an elongated helix-rich fold with a protruding β 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 β 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 β 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.

PubMed: 27152739
DOI: 10.1371/journal.ppat.1005594

Experimental method

X-RAY DIFFRACTION (1.85 Å)