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Literature summary for 3.6.4.B7 extracted from

  • Li, Y.; He, Y.; Luo Y.
    Conservation of a conformational switch in RadA recombinase from Methanococcus maripaludis (2009), Acta Crystallogr. Sect. D, 65, 602-610.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B7

Cloned(Commentary)

Cloned (Comment) Organism
hexagonal MmRadA crystals (space group P61) are grown by the hanging-drop vapour-diffusion method and grew to maximum dimensions of 0.1 x 0.1 x 0.3 mm. Crystal structure of enzyme in complex with AMPPNP, crystal structure of the enzyme in complex with AMPPNP and potassium ions and crystal structure of the enzyme in complex with AMPPNP and ammonium ions Methanococcus maripaludis

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Methanococcus maripaludis

Metals/Ions

Metals/Ions Comment Organism Structure
KCl stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP Methanococcus maripaludis
NH4Cl stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP Methanococcus maripaludis
RbCl stimulates the ssDNA-dependent ATPase activity. 1.0 M RbCl does not stimulate the ATPase activity of MmRadA in the absence of DNA Methanococcus maripaludis

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis P0CW58
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O ssDNA-dependent ATPase activity Methanococcus maripaludis ADP + phosphate
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 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Methanococcus maripaludis