Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function

• Published in: Viruses Vol. 14; no. 10; p. 2215
• Main Authors: Lokareddy, Ravi K., Hou, Chun-Feng David, Li, Fenglin, Yang, Ruoyu, Cingolani, Gino
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.10.2022; MDPI
• Subjects: Adenosine Triphosphate; Amino acids; bacteriophages; Bacteriophages - chemistry; Bacteriophages - genetics; Conserved sequence; cryo-EM; Cryoelectron Microscopy; DNA Packaging; DNA, Viral - chemistry; E coli; Electron microscopy; Endodeoxyribonucleases - genetics; Environmental conditions; Genomes; Herpes viruses; Mechanical properties; Phages; Phylogenetics; Physiological aspects; Protein structure; Proteins; Quaternary structure; Review; Salmonella; Structure; Symmetry; Terminase; terminase subunits; TerS; viral genome packaging; Viral proteins; Viral Proteins - genetics; Virus Assembly - genetics; Virus research; X-ray crystallography; United States; X-ray crystallography; TerS; bacteriophages; herpesviruses; terminase subunits; viral genome packaging; cryo-EM

The genome packaging motor of bacteriophages and herpesviruses is built by two terminase subunits, known as large (TerL) and small (TerS), both essential for viral genome packaging. TerL structure, composition, and assembly to an empty capsid, as well as the mechanisms of ATP-dependent DNA packaging...