Article Abstract:
The crystal structure of T7 gene 4 ring helicase has been found to indicate a mechanism for sequential nucleotide hydrolysis. The crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7 has been determined.
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Article Abstract:
The processing of stalled DNA replication forks, due to DNA damage, is mediated by RecG protein. Data indicate that RecG reverses the fork past the damage and forms a four-way junction, which pemits template switching and lesion bypass.
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Article Abstract:
The helicase domain from the replicative helicase-primase of bacteriophage T7 and its crystal structure are discussed. The structure of the domain and its interactions with nearby subunits in the crystal are like those of the RecA protein. Possible mechanisms for coupling the energy of nucleotide hydrolysis to a change in protein conformation that unwinds DNA are suggested by comparison with RecA and other nucleotide hydrolases with similar structures.
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