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Structure paper

TitleStructures of DNA-bound human ligase IV catalytic core reveal insights into substrate binding and catalysis.
Journal, issue, pagesNat Commun, Vol. 9, Page 2642-2642, Year 2018
Publish dateNov 8, 2017 (structure data deposition date)
AuthorsKaminski, A.M. / Tumbale, P.P. / Schellenberg, M.J. / Williams, R.S. / Williams, J.G. / Kunkel, T.A. / Pedersen, L.C. / Bebenek, K.
External linksNat Commun / PubMed:29980672
MethodsX-ray diffraction
Resolution2.402 - 3.25 Å
Structure data

PDB-6bkf:
Lysyl-adenylate form of human LigIV catalytic domain with bound DNA substrate in open conformation
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

PDB-6bkg:
Human LigIV catalytic domain with bound DNA-adenylate intermediate in closed conformation
Method: X-RAY DIFFRACTION / Resolution: 2.402 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsLIGASE/DNA / DNA double-strand break repair / ligase / nonhomologous end-joining / LIGASE-DNA complex

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