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Literature summary for 2.7.7.7 extracted from

  • Espinoza-Herrera, S.J.; Gaur, V.; Suo, Z.; Carey, P.R.
    Following DNA chain extension and protein conformational changes in crystals of a Y-Family DNA polymerase via Raman crystallography (2013), Biochemistry, 52, 4881.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, crystals of the enzyme in complexes with DNA (the binary complex) in the presence or absence of an incoming nucleotide are analyzed by Raman microscopy. 13C- and 15N-labeled d*CTP, or unlabeled dCTP, are soaked into the binary crystals with G as the templating base. In the presence of the catalytic metal ions, Mg2+ and Mn2+, nucleotide incorporation is detected by the disappearance of the triphosphate band of dCTP and the retention of *C modes in the crystal following soaking out of noncovalently bound C(or *C)TP. The addition of the second coded base, thymine, is observed by adding cognate dTTP to the crystal following a single d*CTP addition. Adding these two bases caused visible damage to the crystal that is possibly caused by protein and/or DNA conformational change within the crystal. When d*CTP is soaked into the Dpo4 crystal in the absence of Mn2+ or Mg2+, the primer extension reaction does not occur. Instead, a ternary protein/template/d*CTP complex is formed Saccharolobus solfataricus

Organism

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

Synonyms Comment Organism
Dpo4
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Saccharolobus solfataricus