The Unusual Fold of Herpes Simplex Virus 1 UL21, a Multifunctional Tegument Protein |
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| Authors: | Claire M Metrick Pooja Chadha Ekaterina E Heldwein |
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| Institution: | aDepartment of Molecular Biology and Microbiology and Graduate Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, Massachusetts, USA;bDepartment of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania, USA |
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| 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. |
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