6M5S

The coordinates of the apo hexameric terminase complex

6M5S の概要

• エントリーDOI: 10.2210/pdb6m5s/pdb
• EMDBエントリー: 30091
• 分子名称: Tripartite terminase subunit 3, Tripartite terminase subunit 1, Tripartite terminase subunit 2, ... (4 entities in total)
• 機能のキーワード: hexamer terminase complex, apo state, viral protein
• 由来する生物種: Human alphaherpesvirus 1 strain 17 (HHV-1); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 174180.55

構造登録者

Yang, Y.X.,Yang, P.,Wang, N.,Chen, Z.H.,Zhou, Z.H.,Rao, Z.H.,Wang, X.X. (登録日: 2020-03-11, 公開日: 2020-10-28, 最終更新日: 2025-07-02)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.9 Å)