Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.102 extracted from

  • Holzer, S.; Yan, J.; Kilkenny, M.; Bell, S.; Pellegrini, L.
    Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster (2017), Nat. Commun., 8, 1718 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.102

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion in sitting drops at 19°C. X-ray crystal structure of heterotrimeric PriSLX from S. solfataricus at 2.9 A resolution Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q9UWW1 AND Q97Z83 AND Q97ZS7 Q9UWW1: DNA primase large subunit PriL, Q97Z83: DNA primase small (catalytic) subunit PriS, Q97ZS7: PriX domain-containing protein
-
Saccharolobus solfataricus ATCC 35092 Q9UWW1 AND Q97Z83 AND Q97ZS7 Q9UWW1: DNA primase large subunit PriL, Q97Z83: DNA primase small (catalytic) subunit PriS, Q97ZS7: PriX domain-containing protein
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Subunits

Subunits Comment Organism
heterotrimer 1 * 35734 (subunit PriS) + 1 * 37598 (subunit PriL) and 1 * 18029 (subunit PriX), calculated from sequence. PriX is essential for primer synthesis and is structurally related to the Fe-S cluster domain of eukaryotic PriL. PriX contains a nucleotide-binding site required for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe-S cluster domain retains wild type levels of primer synthesis Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
PriSLX
-
 Saccharolobus solfataricus