@article{HutinLingTarbouriechetal.2022,
  author    = {Hutin, Stephanie and Ling, Wai Li and Tarbouriech, Nicolas and Schoehn, Guy and Grimm, Clemens and Fischer, Utz and Burmeister, Wim P.},
  title     = {The vaccinia virus DNA helicase structure from combined single-particle cryo-electron microscopy and AlphaFold2 prediction},
  series = {Viruses},
  volume    = {14},
  journal   = {Viruses},
  number    = {10},
  issn      = {1999-4915},
  doi       = {10.3390/v14102206},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-290523},
  year      = {2022},
  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 {\AA} 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.},
  language  = {en}
}
@article{PeissertSauerGrabarczyketal.2020,
  author    = {Peissert, Stefan and Sauer, Florian and Grabarczyk, Daniel B. and Braun, Cathy and Sander, Gudrun and Poterszman, Arnaud and Egly, Jean-Marc and Kuper, Jochen and Kisker, Caroline},
  title     = {In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair},
  series = {Nature Communications},
  volume    = {11},
  journal   = {Nature Communications},
  number    = {1},
  doi       = {10.1038/s41467-020-15241-9},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-229857},
  year      = {2020},
  abstract  = {The XPD helicase is a central component of the general transcription factor TFIIH which plays major roles in transcription and nucleotide excision repair (NER). Here we present the high-resolution crystal structure of the Arch domain of XPD with its interaction partner MAT1, a central component of the CDK activating kinase complex. The analysis of the interface led to the identification of amino acid residues that are crucial for the MAT1-XPD interaction. More importantly, mutagenesis of the Arch domain revealed that these residues are essential for the regulation of (i) NER activity by either impairing XPD helicase activity or the interaction of XPD with XPG; (ii) the phosphorylation of the RNA polymerase II and RNA synthesis. Our results reveal how MAT1 shields these functionally important residues thereby providing insights into how XPD is regulated by MAT1 and defining the Arch domain as a major mechanistic player within the XPD scaffold.},
  language  = {en}
}