Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein.
AUTOR(ES)
Bird, L E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=146783Documentos Relacionados
- The arginine finger of bacteriophage T7 gene 4 helicase: Role in energy coupling
- Interaction of adjacent primase domains within the hexameric gene 4 helicase-primase of bacteriophage T7
- Roles of bacteriophage T7 gene 4 proteins in providing primase and helicase functions in vivo.
- A 7-kDa region of the bacteriophage T7 gene 4 protein is required for primase but not for helicase activity.
- Gene 4 helicase of bacteriophage T7 mediates strand transfer through pyrimidine dimers, mismatches, and nonhomologous regions