8APL

Vaccinia virus DNA helicase D5 residues 323-785 hexamer with bound DNA processed in C6

8APL の概要

• エントリーDOI: 10.2210/pdb8apl/pdb
• EMDBエントリー: 15574
• 分子名称: Primase D5 (1 entity in total)
• 機能のキーワード: dna helicase, d5_n domain, duf5906 domain, pox_d5 domain, sf3 helicase, viral protein
• 由来する生物種: Vaccinia virus Copenhagen
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 320971.71

構造登録者

Burmeister, W.P.,Hutin, S.,Ling, W.L.,Grimm, C.,Schoehn, G. (登録日: 2022-08-10, 公開日: 2022-11-09, 最終更新日: 2024-07-24)

主引用文献

Hutin, S.,Ling, W.L.,Tarbouriech, N.,Schoehn, G.,Grimm, C.,Fischer, U.,Burmeister, W.P.
The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.
Viruses, 14:-, 2022

PubMed Abstract: Poxviruses are large DNA viruses with a linear double-stranded DNA genome circularized at the extremities. The helicase-primase D5, composed of six identical 90 kDa subunits, is required for DNA replication. D5 consists of a primase fragment flexibly attached to the hexameric C-terminal polypeptide (res. 323-785) with confirmed nucleotide hydrolase and DNA-binding activity but an elusive helicase activity. We determined its structure by single-particle cryo-electron microscopy. It displays an AAA+ helicase core flanked by N- and C-terminal domains. Model building was greatly helped by the predicted structure of D5 using AlphaFold2. The 3.9 Å structure of the N-terminal domain forms a well-defined tight ring while the resolution decreases towards the C-terminus, still allowing the fit of the predicted structure. The N-terminal domain is partially present in papillomavirus E1 and polyomavirus LTA helicases, as well as in a bacteriophage NrS-1 helicase domain, which is also closely related to the AAA+ helicase domain of D5. Using the Pfam domain database, a D5_N domain followed by DUF5906 and Pox_D5 domains could be assigned to the cryo-EM structure, providing the first 3D structures for D5_N and Pox_D5 domains. The same domain organization has been identified in a family of putative helicases from large DNA viruses, bacteriophages, and selfish DNA elements.

PubMed: 36298761
DOI: 10.3390/v14102206

実験手法

ELECTRON MICROSCOPY (4.1 Å)