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TitlePCNA directs type 2 RNase H activity on DNA replication and repair substrates.
Journal, issue, pagesNucleic Acids Res., Vol. 39, Page 3652-3666, Year 2011
Publish dateOct 13, 2010 (structure data deposition date)
AuthorsBubeck, D. / Reijns, M.A. / Graham, S.C. / Astell, K.R. / Jones, E.Y. / Jackson, A.P.
External linksNucleic Acids Res. / PubMed:21245041
MethodsX-ray diffraction
Resolution2.99 - 3.05 Å
Structure data

PDB-3p83:
Structure of the PCNA:RNase HII complex from Archaeoglobus fulgidus.
Method: X-RAY DIFFRACTION / Resolution: 3.05 Å

PDB-3p87:
Structure of human PCNA bound to RNASEH2B PIP box peptide
Method: X-RAY DIFFRACTION / Resolution: 2.99 Å

Source
  • archaeoglobus fulgidus (archaea)
  • homo sapiens (human)
KeywordsHYDROLASE/DNA BINDING PROTEIN / DNA clamp / RNase H fold / cleaves RNA/DNA hybrids / nucleus / HYDROLASE-DNA BINDING PROTEIN complex / DNA binding / DNA replication / DNA repair / sliding clamp / PCNA Peptide Interacting Peptide (PIP) motif / PIP-box motif / processivity factor / RNase H2 / FEN-1 / Ligase / polymerases / helicases / nucleases

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