Unknown

Dataset Information

0

Crystal Structure of Human Herpesvirus 6B Tegument Protein U14.


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 ? 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 ? 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 ? 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.

SUBMITTER: Wang B 

PROVIDER: S-EPMC4859480 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal Structure of Human Herpesvirus 6B Tegument Protein U14.

Wang Bochao B   Nishimura Mitsuhiro M   Tang Huamin H   Kawabata Akiko A   Mahmoud Nora F NF   Khanlari Zahra Z   Hamada Daizo D   Tsuruta Hiroki H   Mori Yasuko Y  

PLoS pathogens 20160506 5


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 crysta  ...[more]

Similar Datasets

| S-EPMC6877594 | biostudies-literature
| S-EPMC10868460 | biostudies-literature
| S-EPMC4019128 | biostudies-literature
| S-EPMC8139660 | biostudies-literature
| S-EPMC112820 | biostudies-literature
| S-EPMC4577881 | biostudies-literature
| S-EPMC1880851 | biostudies-literature
| S-EPMC8068176 | biostudies-literature
| S-EPMC2516262 | biostudies-literature
| S-EPMC5640841 | biostudies-literature