Literature summary for 2.7.7.101 extracted from

Zhou, Y.; Luo, H.; Liu, Z.; Yang, M.; Pang, X.; Sun, F.; Wang, G.
Structural insight into the specific DNA template binding to DnaG primase in bacteria (2017), Sci. Rep., 7, 659 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the RNA polymerase domain of DnaG. The tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. The ssDNA template binding surface is L-shaped, a model for the template ssDNA binding to primase is proposed. Comparison with the enzyme from Geobacillus stearothermophilus	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
K232A	more than 50% decrease in DNA binding activity	Bacillus subtilis
N235A	loss of DNA binding activity	Bacillus subtilis
R148A	mutation slightly affects DNA binding activity	Bacillus subtilis
R202A	mutation significantly affects DNA binding activity	Bacillus subtilis
R204A	mutation significantly affects DNA binding activity	Bacillus subtilis
R224A	more than 50% decrease in DNA binding activity	Bacillus subtilis
W167A	mutation significantly affects DNA binding activity	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P05096	-	-
Bacillus subtilis 168	P05096	-	-

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Release 2023.1 (January 2023)