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Structure paper

TitleArchitecture of the herpesvirus genome-packaging complex and implications for DNA translocation.
Journal, issue, pagesProtein Cell, Vol. 11, Issue 5, Page 339-351, Year 2020
Publish dateApr 23, 2020
AuthorsYunxiang Yang / Pan Yang / Nan Wang / Zhonghao Chen / Dan Su / Z Hong Zhou / Zihe Rao / Xiangxi Wang /
PubMed AbstractGenome packaging is a fundamental process in a viral life cycle and a prime target of antiviral drugs. Herpesviruses use an ATP-driven packaging motor/terminase complex to translocate and cleave ...Genome packaging is a fundamental process in a viral life cycle and a prime target of antiviral drugs. Herpesviruses use an ATP-driven packaging motor/terminase complex to translocate and cleave concatemeric dsDNA into procapsids but its molecular architecture and mechanism are unknown. We report atomic structures of a herpesvirus hexameric terminase complex in both the apo and ADP•BeF3-bound states. Each subunit of the hexameric ring comprises three components-the ATPase/terminase pUL15 and two regulator/fixer proteins, pUL28 and pUL33-unlike bacteriophage terminases. Distal to the nuclease domains, six ATPase domains form a central channel with conserved basic-patches conducive to DNA binding and trans-acting arginine fingers are essential to ATP hydrolysis and sequential DNA translocation. Rearrangement of the nuclease domains mediated by regulatory domains converts DNA translocation mode to cleavage mode. Our structures favor a sequential revolution model for DNA translocation and suggest mechanisms for concerted domain rearrangements leading to DNA cleavage.
External linksProtein Cell / PubMed:32328903 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.5 Å
Structure data

30090

6m5r

EMDB-30090, PDB-6m5r:
The coordinates of the apo monomeric terminase complex
Method: EM (single particle) / Resolution: 3.5 Å

30091

6m5s

EMDB-30091, PDB-6m5s:
The coordinates of the apo hexameric terminase complex
Method: EM (single particle) / Resolution: 3.9 Å

30092

6m5t

EMDB-30092, PDB-6m5t:
The coordinate of the nuclease domain of the apo terminase complex
Method: EM (single particle) / Resolution: 3.6 Å

30093

6m5u

EMDB-30093, PDB-6m5u:
The coordinates of the monomeric terminase complex in the presence of the ADP-BeF3
Method: EM (single particle) / Resolution: 3.8 Å

30094

6m5v

EMDB-30094, PDB-6m5v:
The coordinate of the hexameric terminase complex in the presence of the ADP-BeF3
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

Source
  • human alphaherpesvirus 1 strain 17
  • Human herpesvirus 1 (Herpes simplex virus type 1)
  • human herpesvirus 1 (strain 17)
KeywordsVIRAL PROTEIN / HSV-1 / terminase complex / apo state / hexamer terminase complex / nuclease domain / apo terminase complex / ADP-BeF3 / monomer

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