Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein

Nucleic Acids Res. 1997 Jul 1;25(13):2620-6. doi: 10.1093/nar/25.13.2620.

Abstract

Limited proteolysis of bacteriophage T7 primase/helicase with endoproteinase Glu-C produces several proteolytic fragments. One of these fragments, which is derived from the C-terminal region of the protein, was prepared and shown to retain helicase activity. This result supports a model in which the gene 4 proteins consist of functionally separable domains. Crystals of this C-terminal fragment of the protein have been obtained that are suitable for X-ray diffraction studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • DNA Helicases / chemistry*
  • DNA Primase
  • Hydrolysis
  • Kinetics
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • RNA Nucleotidyltransferases / chemistry*
  • Serine Endopeptidases / metabolism
  • Thymine Nucleotides / metabolism

Substances

  • Peptide Fragments
  • Thymine Nucleotides
  • DNA Primase
  • RNA Nucleotidyltransferases
  • Serine Endopeptidases
  • glutamyl endopeptidase
  • DNA Helicases
  • thymidine 5'-triphosphate