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Structure paper

TitleStructural basis of DNA packaging by a ring-type ATPase from an archetypal viral system.
Journal, issue, pagesNucleic Acids Res, Vol. 50, Issue 15, Page 8719-8732, Year 2022
Publish dateAug 26, 2022
AuthorsHerman 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 AbstractMany 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 linksNucleic Acids Res / PubMed:35947691 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.4 - 22.0 Å
Structure data

EMDB-22099:
HK97 prohead during packaging (sym5)
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-22100:
Hk97 prohead during packaging (sym6)
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-22101:
prohead of HK97 for packaging
Method: EM (single particle) / Resolution: 6.9 Å

PDB-6z6d:
Crystal structure of the HK97 bacteriophage large terminase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6z6e:
Crystal structure of the HK97 bacteriophage small terminase
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-BR:
BROMIDE ION

ChemComp-HOH:
WATER

ChemComp-IOD:
IODIDE ION

Source
  • enterobacteria phage hk97 (virus)
KeywordsVIRAL PROTEIN / genome packaging / bacteriophage / ATPase / nuclease / DNA binding

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