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TitleCombined Solution and Crystal Methods Reveal the Electrostatic Tethers That Provide a Flexible Platform for Replication Activities in the Bacteriophage T7 Replisome.
Journal, issue, pagesBiochemistry, Vol. 58, Page 4466-4479, Year 2019
Publish dateJun 5, 2019 (structure data deposition date)
AuthorsFoster, B.M. / Rosenberg, D. / Salvo, H. / Stephens, K.L. / Bintz, B.J. / Hammel, M. / Ellenberger, T. / Gainey, M.D. / Wallen, J.R.
External linksBiochemistry / PubMed:31659895
MethodsX-ray diffraction
Resolution3.001 Å
Structure data

PDB-6p7e:
Structure of T7 DNA Polymerase Bound to a Primer/Template DNA and a Peptide that Mimics the C-terminal Tail of the Primase-Helicase
Method: X-RAY DIFFRACTION / Resolution: 3.001 Å

Chemicals

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t7 (virus)
  • escherichia coli (E. coli)
KeywordsTRANSFERASE/DNA BINDING PROTEIN/DNA / DNA Replication / DNA polymerase / DNA binding protein / TRANSFERASE-DNA BINDING PROTEIN-DNA complex

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