5ED7

Crystal Structure of HSV-1 UL21 C-terminal Domain

Summary for 5ED7

• Entry DOI: 10.2210/pdb5ed7/pdb
• Related: 4U4H
• Descriptor: Tegument protein UL21, CHLORIDE ION (3 entities in total)
• Functional Keywords: viral protein
• Biological source: Human herpesvirus 1 (strain 17) (HHV-1)
• Total number of polymer chains: 1
• Total formula weight: 27569.08

Authors

Metrick, C.M.,Heldwein, E.E. (deposition date: 2015-10-20, release date: 2016-04-20, Last modification date: 2024-03-06)

Primary citation

Metrick, C.M.,Heldwein, E.E.
Novel Structure and Unexpected RNA-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein UL21.
J.Virol., 90:5759-5769, 2016

PubMed Abstract: Proteins forming the tegument layers of herpesviral virions mediate many essential processes in the viral replication cycle, yet few have been characterized in detail. UL21 is one such multifunctional tegument protein and is conserved among alphaherpesviruses. While UL21 has been implicated in many processes in viral replication, ranging from nuclear egress to virion morphogenesis to cell-cell spread, its precise roles remain unclear. Here we report the 2.7-Å crystal structure of the C-terminal domain of herpes simplex virus 1 (HSV-1) UL21 (UL21C), which has a unique α-helical fold resembling a dragonfly. Analysis of evolutionary conservation patterns and surface electrostatics pinpointed four regions of potential functional importance on the surface of UL21C to be pursued by mutagenesis. In combination with the previously determined structure of the N-terminal domain of UL21, the structure of UL21C provides a 3-dimensional framework for targeted exploration of the multiple roles of UL21 in the replication and pathogenesis of alphaherpesviruses. Additionally, we describe an unanticipated ability of UL21 to bind RNA, which may hint at a yet unexplored function.

PubMed: 27053559
DOI: 10.1128/JVI.00475-16

Experimental method

X-RAY DIFFRACTION (2.72 Å)