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

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.

SUBMITTER: Bird LE

PROVIDER: S-EPMC146783 | biostudies-other | 1997 Jul

REPOSITORIES: biostudies-other

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

Bird L E LE Hâkansson K K Pan H H Wigley D B DB

Nucleic acids research 19970701 13

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. ...[more]

PMID: 9185573

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