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-Structure paper
Title | Structural basis of DNA packaging by a ring-type ATPase from an archetypal viral system. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 50, Issue 15, Page 8719-8732, Year 2022 |
Publish date | Aug 26, 2022 |
Authors | Herman K H Fung / Shelley Grimes / Alexis Huet / Robert L Duda / Maria Chechik / Joseph Gault / Carol V Robinson / Roger W Hendrix / Paul J Jardine / James F Conway / Christoph G Baumann / Alfred A Antson / |
PubMed Abstract | Many essential cellular processes rely on substrate rotation or translocation by a multi-subunit, ring-type NTPase. A large number of double-stranded DNA viruses, including tailed bacteriophages and ...Many essential cellular processes rely on substrate rotation or translocation by a multi-subunit, ring-type NTPase. A large number of double-stranded DNA viruses, including tailed bacteriophages and herpes viruses, use a homomeric ring ATPase to processively translocate viral genomic DNA into procapsids during assembly. Our current understanding of viral DNA packaging comes from three archetypal bacteriophage systems: cos, pac and phi29. Detailed mechanistic understanding exists for pac and phi29, but not for cos. Here, we reconstituted in vitro a cos packaging system based on bacteriophage HK97 and provided a detailed biochemical and structural description. We used a photobleaching-based, single-molecule assay to determine the stoichiometry of the DNA-translocating ATPase large terminase. Crystal structures of the large terminase and DNA-recruiting small terminase, a first for a biochemically defined cos system, reveal mechanistic similarities between cos and pac systems. At the same time, mutational and biochemical analyses indicate a new regulatory mechanism for ATPase multimerization and coordination in the HK97 system. This work therefore establishes a framework for studying the evolutionary relationships between ATP-dependent DNA translocation machineries in double-stranded DNA viruses. |
External links | Nucleic Acids Res / PubMed:35947691 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.4 - 22.0 Å |
Structure data | EMDB-22099: EMDB-22100: EMDB-22101: PDB-6z6d: PDB-6z6e: |
Chemicals | ChemComp-BR: ChemComp-HOH: ChemComp-IOD: |
Source |
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Keywords | VIRAL PROTEIN / genome packaging / bacteriophage / ATPase / nuclease / DNA binding |