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Structure paper

TitleT4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction.
Journal, issue, pagesNucleic Acids Res., Vol. 46, Page 10474-10488, Year 2018
Publish dateJul 13, 2017 (structure data deposition date)
AuthorsShi, K. / Bohl, T.E. / Park, J. / Zasada, A. / Malik, S. / Banerjee, S. / Tran, V. / Li, N. / Yin, Z. / Kurniawan, F. ...Shi, K. / Bohl, T.E. / Park, J. / Zasada, A. / Malik, S. / Banerjee, S. / Tran, V. / Li, N. / Yin, Z. / Kurniawan, F. / Orellana, K. / Aihara, H.
External linksNucleic Acids Res. / PubMed:30169742
MethodsX-ray diffraction
Resolution1.4 - 2.75 Å
Structure data

PDB-5wfy:
Crystal structure of DNA-binding domain of the bacteriophage T4 ligase
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6drt:
Crystal structure of the processivity clamp GP45 complexed with recognition peptide of ligase from bacteriophage T4
Method: X-RAY DIFFRACTION / Resolution: 2.117 Å

PDB-6dt1:
Crystal structure of the ligase from bacteriophage T4 complexed with DNA intermediate
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-DTT:
2,3-DIHYDROXY-1,4-DITHIOBUTANE

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • enterobacteria phage t4 (virus)
KeywordsLIGASE / LIGASE-DNA COMPLEX / GENE REGULATION / HYDROLASE / processivity clamp / LIGASE/DNA

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