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Literature summary extracted from

  • Rymer, R.; Solorio, F.; Tehranchi, A.; Chu, C.; Corn, J.; Keck, J.; Wang, J.; Berger, J.
    Binding mechanism of metal-NTP substrates and stringent-response alarmones to bacterial DnaG-type primases (2012), Structure, 20, 1478-1489 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.101 structures of the DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.101 ppGpp inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex Escherichia coli
2.7.7.101 ppGpp inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex Staphylococcus aureus
2.7.7.101 pppGpp inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex Escherichia coli
2.7.7.101 pppGpp inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.101 Escherichia coli P0ABS5
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2.7.7.101 Staphylococcus aureus O05338
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