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Literature summary 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)

EC Number Crystallization (Comment) Organism
2.7.7.101 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

EC Number Organism UniProt Comment Textmining
2.7.7.101 Mycobacterium tuberculosis
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2.7.7.101 Mycobacterium tuberculosis H37Rv
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General Information

EC Number General Information Comment Organism
2.7.7.101 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