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Literature summary for 2.7.7.102 extracted from

  • Vaithiyalingam, S.; Arnett, D.R.; Aggarwal, A.; Eichman, B.F.; Fanning, E.; Chazin, W.J.
    Insights into eukaryotic primer synthesis from structures of the p48 subunit of human DNA primase (2014), J. Mol. Biol., 426, 558-569 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Mn2+ significantly enhances the binding of nucleotide to primase,which correlates with higher catalytic efficiency in vitro Homo sapiens
additional information not activating: Mg2+ Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
strcuture of the highly conserved C-terminal regulatory domain of the large subunit to 1.7 A resolution. The evolutionarily conserved 4Fe-4S cluster is buried deeply within the protein core. DNA binding shows a strong preference for ss/dsDNA junction substrates. The enzyme interacts specifically with the C-terminal domain of the intermediate subunit of replication protein A, RPA32C Homo sapiens
structure of the catalytic subunit, with bound UTP and Mn2+. Primase contains the conserved catalytic prim fold domain, with a subdomain different from the archaeal and bacterial primases. Residues S160 and H166 are in direct contact with UTP Homo sapiens

Protein Variants

Protein Variants Comment Organism
D111N residue is essential for viability Saccharomyces cerevisiae
D113N residue is essential for viability Saccharomyces cerevisiae
D314N residue is essential for viability Saccharomyces cerevisiae
H168A residue is essential for viability Saccharomyces cerevisiae
H299D 10fold reduction in affinity for replication protein A Homo sapiens
H323A residue is essential for viability Saccharomyces cerevisiae
K326A residue is essential for viability Saccharomyces cerevisiae
R164A residue is essential for viability Saccharomyces cerevisiae
R165A residue is essential for viability Saccharomyces cerevisiae
R302 50fold reduction in affinity for replication protein A Homo sapiens
S162A residue is essential for viability Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Homo sapiens P49642 subunit Prim1
-
Homo sapiens P49642 and P49643 P49642 i.e. subunit Prim1, P49643 i.e. large subunit Prim2
-
Saccharomyces cerevisiae P10363 subunit Pri1
-

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center cluster is buried deeply within the protein core Homo sapiens