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-Structure paper
タイトル | Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation. |
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ジャーナル・号・ページ | Protein Cell, Vol. 11, Issue 5, Page 339-351, Year 2020 |
掲載日 | 2020年4月23日 |
![]() | Yunxiang Yang / Pan Yang / Nan Wang / Zhonghao Chen / Dan Su / Z Hong Zhou / Zihe Rao / Xiangxi Wang / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.5 - 4.5 Å |
構造データ | EMDB-30090, PDB-6m5r: EMDB-30091, PDB-6m5s: EMDB-30092, PDB-6m5t: EMDB-30093, PDB-6m5u: EMDB-30094, PDB-6m5v: |
化合物 | ![]() ChemComp-ZN: ![]() ChemComp-ADP: ![]() ChemComp-BEF: ![]() ChemComp-MG: |
由来 |
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![]() | VIRAL PROTEIN / HSV-1 / terminase complex / apo state / hexamer terminase complex / nuclease domain / apo terminase complex / ADP-BeF3 / monomer |