4U4H

Crystal Structure of HSV-1 UL21 N-terminal Domain

Summary for 4U4H

Entry DOI	10.2210/pdb4u4h/pdb
Descriptor	Tegument protein UL21 (2 entities in total)
Functional Keywords	viral protein
Biological source	Human herpesvirus 1 (HHV-1)
Cellular location	Virion tegument: P10205
Total number of polymer chains	1
Total formula weight	23180.26
Authors	Metrick, C.M.,Heldwein, E.E. (deposition date: 2014-07-23, release date: 2015-01-07, Last modification date: 2023-12-27)
Primary citation	Metrick, C.M.,Chadha, P.,Heldwein, E.E. The Unusual Fold of Herpes Simplex Virus 1 UL21, a Multifunctional Tegument Protein. J.Virol., 89:2979-2984, 2015 Cited by PubMed Abstract: UL21 is a conserved protein in the tegument of alphaherpesviruses and has multiple important albeit poorly understood functions in viral replication and pathogenesis. To provide a roadmap for exploration of the multiple roles of UL21, we determined the crystal structure of its conserved N-terminal domain from herpes simplex virus 1 to 2.0-Å resolution, which revealed a novel sail-like protein fold. Evolutionarily conserved surface patches highlight residues of potential importance for future targeting by mutagenesis. PubMed: 25540382 DOI: 10.1128/JVI.03516-14 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.05 Å)

Structure validation