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Structure paper

TitleStructures of bacterial polynucleotide kinase in a Michaelis complex with GTP*Mg2+ and 5'-OH oligonucleotide and a product complex with GDP*Mg2+ and 5'-PO4 oligonucleotide reveal a mechanism of general acid-base catalysis and the determinants of phosphoacceptor recognition.
Journal, issue, pagesNucleic Acids Res., Vol. 42, Page 1152-1161, Year 2014
Publish dateAug 22, 2013 (structure data deposition date)
AuthorsDas, U. / Wang, L.K. / Smith, P. / Jacewicz, A. / Shuman, S.
External linksNucleic Acids Res. / PubMed:24150947
MethodsX-ray diffraction
Resolution1.727 - 1.8 Å
Structure data

PDB-4mde:
Structure of bacterial polynucleotide kinase product complex bound to GDP and DNA
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4mdf:
Structure of bacterial polynucleotide kinase Michaelis complex bound to GTP and DNA
Method: X-RAY DIFFRACTION / Resolution: 1.727 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-CIT:
CITRIC ACID

Source
  • clostridium thermocellum (bacteria)
KeywordsTRANSFERASE/DNA / RNA repair / P-loop phosphotransferase / transferase / HYDROLASE-DNA complex / TRANSFERASE-DNA complex

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