Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein.
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.
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Laboratory of Molecular Biophysics, Rex Richards Building, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Hâkansson
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D000595:Amino Acid Sequence; D003460:Crystallization; D004265:DNA Helicases / Q000737:chemistry*; D019915:DNA Primase; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D012316:RNA Nucleotidyltransferases / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000378:metabolism; D013942:Thymine Nucleotides / Q000378:metabolism
D010446:Peptide Fragments; D013942:Thymine Nucleotides; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D004265:DNA Helicases; C024157:thymidine 5'-triphosphate