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The phage tail-like tubule of the T6SS assembles on a structure analogous to bacteriophage baseplates. It consists of the proteins TssE, TssF, TssG, and TssK. The baseplate and phage tail-like complex interact in the bacterial cytoplasm, and then are recruited to the cell envelope by the membrane complex. [10]
In molecular biology, bacteriophage scaffolding proteins are proteins involved in bacteriophage assembly. The assembly of a macromolecular structure proceeds via a specific pathway of ordered events and involves conformational changes in the proteins as they join the assembly. The assembly process is aided by scaffolding proteins, which act as ...
In molecular biology, the Cro repressor family is a family of repressor proteins in bacteriophage lambda that includes the Cro repressor.. Bacteriophage lambda encodes two repressors: the Cro repressor that acts to turn off early gene transcription during the lytic cycle, and the lambda or cI repressor required to maintain lysogenic growth.
Structural model at atomic resolution of bacteriophage T4 [1] The structure of a typical myovirus bacteriophage Anatomy and infection cycle of bacteriophage T4. A bacteriophage (/ b æ k ˈ t ɪər i oʊ f eɪ dʒ /), also known informally as a phage (/ ˈ f eɪ dʒ /), is a virus that infects and replicates within bacteria and archaea.
However, some tailed bacteriophage genomes can vary quite significantly in nucleotide sequence, even among the same genus. Due to their characteristic structure and possession of potentially homologous genes, it is believed these bacteriophages possess a common origin.
Bacteriophage Lambda binds to an E. coli cell by means of its J protein in the tail tip. The J protein interacts with the maltose outer membrane porin (the product of the lamB gene) of E. coli, [9] a porin molecule, which is part of the maltose operon. The linear phage genome is injected through the outer membrane.
Phage display cycle. 1) fusion proteins for a viral coat protein + the gene to be evolved (typically an antibody fragment) are expressed in bacteriophage. 2) the library of phage are washed over an immobilised target. 3) the remaining high-affinity binders are used to infect bacteria. 4) the genes encoding the high-affinity binders are isolated.
structure summary In molecular biology , a phage major coat protein is an alpha-helical protein that forms a viral envelope of filamentous bacteriophages . These bacteriophages are flexible rods, about one to two micrometres long and six nm in diameter, with a helical shell of protein subunits surrounding a DNA core.