Literature summary for 2.7.7.7 extracted from

Sun, S.; Geng, L.; Shamoo, Y.
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity (2006), Proteins, 65, 231-238.

Search for more literature for 2.7.7.7

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of RB69 single-stranded DNA binding protein-DNA polymerase fusion	Escherichia phage RB69

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of this fusion protein is solved by a combination of multiwavelength anomalous diffraction and molecular replacement to 3.2 A resolution and shows that RB69 single-stranded DNA binding protein is positioned proximal to the N-terminal domain of RB69 DNA polymerase near the template strand channel	Escherichia phage RB69

Protein Variants

Protein Variants	Comment	Organism
additional information	fusion of RB69 DNA polymerase with its cognate single-stranded DNA binding protein via a short six amino acid linker increases affinity for primer-template DNA by 6fold and subsequently increases processivity by 7fold while maintaining fidelity	Escherichia phage RB69

Organism

Organism	UniProt	Comment	Textmining
Escherichia phage RB69	-	-	-

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Release 2023.1 (January 2023)