Literature summary for 2.7.7.7 extracted from

Kirouac, K.N.; Suo, Z.; Ling, H.
Structural mechanism of ribonucleotide discrimination by a Y-family DNA polymerase (2011), J. Mol. Biol., 407, 382-390.

Search for more literature for 2.7.7.7

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal forms for the N249Y mutant enzyme are obtained at 22°C by the microbatch method	Saccharolobus solfataricus

Protein Variants

Protein Variants	Comment	Organism
N249Y	exhibits increased catalytic activity when compared to the wild-type enzyme, the mutation decreases the affinity for NAD(H) cofactor	Saccharolobus solfataricus
Y12A	active-site mutation Y12A in Dpo4, causes both a dramatic loss of ribonucleotide discrimination and a decrease in nucleotide incorporation efficiency	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q97W02	-	-
Saccharolobus solfataricus P2	Q97W02	-	-

Synonyms

Synonyms	Comment	Organism
Dpo4	-	Saccharolobus solfataricus

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Release 2023.1 (January 2023)