Crystallization (Comment) | Organism |
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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 | Comment | Organism | Structure |
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Mn2+ | in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain | Sulfolobus islandicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus islandicus | - |
- |
- |
Purification (Comment) | Organism |
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- |
Sulfolobus islandicus |
Synonyms | Comment | Organism |
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DNA primase-polymerase | bifunctiional enzyme | Sulfolobus islandicus |