The C-terminal domain of ToIA is the coreceptor for filamentous phage infection of E. coli

Article Abstract:

A study was conducted to identify the C-terminal domain of the periplasmic protein ToIA as the coreceptor for infection of Escherichia coli by phage fd and the N-terminal domain of the phage minor coat protein g3p as the cognate ligand. The results indicate a sequential two-way docking mechanism for phage infection, analogous to infection pathways proposed for eukaryotic viruses.

Cell receptors, Escherichia coli infections

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Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69

Article Abstract:

A study was conducted on the crystal structure of a pol alpha family replication DNA polymerase form bacteriophage RB69. Results show that although 2.8 A resolution crystal structure of the bacteriophage have similar features with other polymerases, they also exhibit several differences. This include is the location of one the three carboxylates needed for nucleotidyl transfer.

DNA polymerases

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