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Structure paper

TitleMolecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page 13248-13253, Year 2012
Publish dateFeb 16, 2012 (structure data deposition date)
AuthorsWang, P. / Chan, C.M. / Christensen, D. / Zhang, C. / Selvadurai, K. / Huang, R.H.
External linksProc. Natl. Acad. Sci. USA / PubMed:22847431
MethodsX-ray diffraction
Resolution2.301 - 2.6 Å
Structure data

PDB-4dqz:
Crystal Structure of C-terminal Half of Bacterial Hen1
Method: X-RAY DIFFRACTION / Resolution: 2.301 Å

PDB-4drf:
Crystal Structure of Bacterial Pnkp-C/Hen1-N Heterodimer
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4e6n:
Crystal structure of bacterial Pnkp-C/Hen1-N heterodimer
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • clostridium thermocellum (bacteria)
KeywordsTRANSFERASE / Ligase-activating / Bacterial Pnkp / PROTEIN BINDING / RNA repair / RNA ligase

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