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2.7.7.B16: DNA primase

This is an abbreviated version!
For detailed information about DNA primase, go to the full flat file.

Word Map on EC 2.7.7.B16

Reaction

dNTP
+ n dNTP =
dN(pdN)n
 + n diphosphate

Synonyms

archaeal eukaryotic-type primase, DNA primase-polymerase, DnaG primase, Mjpri, Pabp41, Pabp46, pIT3 replication protein, PolpTN2, PriL, PriS, PriSL, PriX, Sso core primase, SsoPriSL

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B16 DNA primase

Crystallization

Crystallization on EC 2.7.7.B16 - DNA primase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion in sitting drops at 20°C. Crystal structure of the catalytic primase subunit, 2.3 A resolution
Q9P9H1; Q8U4H7
cocrystalization with uridine 5'-triphosphate allowing confirmation of the location of the active site. Construction of a model between the DNA primase and a primer/template DNA based on the complex structure for the primer synthesis
crystallographic studies of of the N-terminal domain (NTD) of PriL (PriLNTD; residues 1–222) that bind to PriS, 2.9 A resolution
hanging-drop vapor diffusion method at 20°C, with polyethylene glycol 8000 as the precipitant. The crystals belong to the P3(2)21 with unit-cell parameters a = b = 77.8, c = 129.6 A, and alpha = beta = 90°, gamma = 120°. Crystals of the selenomethionine derivative are obtained by means of a cross-seeding method using native crystals. The data for the native and selenomethionine-substituted crystals are collected to 1.8 and 2.2 A resolution
hanging drop vapor diffusion at 18°C, the structure provides the first three-dimensional description of the large subunit and its interaction with the small subunit
purified recombinant PriX deletion mutant 26-154, X-ray diffraction strutcure determination and analysis at 1.95 A resolution, crystallization of the full-length PriX is unsuccessful
Q9UWW1; Q97Z83; Q97ZS7
structure-function analysis of the pRN1 primase-polymerase domain. The crystal structure shows a central depression lined by conserved residues. Mutations on one side of the depression reduce DNA affinity. On the opposite side of the depression cluster three acidic residues and a histidine, which are required for primase and DNA polymerase activity. One acidic residue binds a manganese ion, suggestive of a metal-dependent catalytic mechanism. The structure does not show any similarity to DNA polymerases, but is distantly related to archaeal and eukaryotic primases, with corresponding active-site residues
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