Literature summary for 2.7.7.101 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 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Inhibitors	Comment	Organism	Structure
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
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
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
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

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABS5	-	-
Staphylococcus aureus	O05338	-	-

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Release 2023.1 (January 2023)