6M5T

The coordinate of the nuclease domain of the apo terminase complex

Summary for 6M5T

• Entry DOI: 10.2210/pdb6m5t/pdb
• EMDB information: 30092
• Descriptor: Tripartite terminase subunit 3 (1 entity in total)
• Functional Keywords: hsv-1, nuclease domain, apo terminase complex, viral protein
• Biological source: Human alphaherpesvirus 1 strain 17 (HHV-1)
• Total number of polymer chains: 1
• Total formula weight: 30918.91

Authors

Yang, Y.X.,Yang, P.,Wang, N.,Chen, Z.H.,Zhou, Z.H.,Rao, Z.H.,Wang, X.X. (deposition date: 2020-03-11, release date: 2020-10-28, Last modification date: 2025-07-02)

Primary citation

Yang, Y.,Yang, P.,Wang, N.,Chen, Z.,Su, D.,Zhou, Z.H.,Rao, Z.,Wang, X.
Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation.
Protein Cell, 11:339-351, 2020

PubMed Abstract: 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.

PubMed: 32328903
DOI: 10.1007/s13238-020-00710-0

Experimental method

ELECTRON MICROSCOPY (3.6 Å)