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

BRENDA support

Literature summary for 2.7.7.101 extracted from

  • Hou, C.; Biswas, T.; Tsodikov, O.V.
    Structures of the catalytic domain of bacterial primase DnaG in complexes with DNA provide insight into key priming events (2018), Biochemistry, 57, 2084-2093 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of noncovalent DnaG-DNA complexes, of the RNA polymerase domain of DnaG and various DNA ligands. A key site for DnaG interaction with ds/ss DNA, located on the N-terminal subdomain of the RNAS polymerase domain Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-

General Information

General Information Comment Organism
physiological function model of the RNA polymerase domain bound to the primed template. As the template strand exits the binding site on the primase on the 5'-side it enters the active site of the DNA polymerase in a proper polarity Mycobacterium tuberculosis