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Literature summary for 2.7.7.B16 extracted from

  • Lipps, G.; Weinzierl, A.O.; von Scheven, G.; Buchen, C.; Cramer, P.
    Structure of a bifunctional DNA primase-polymerase (2004), Nat. Struct. Mol. Biol., 11, 157-162.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Sulfolobus islandicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain Sulfolobus islandicus

Organism

Organism UniProt Comment Textmining
Sulfolobus islandicus
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfolobus islandicus

Synonyms

Synonyms Comment Organism
DNA primase-polymerase bifunctiional enzyme Sulfolobus islandicus