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Literature summary for 3.6.4.B7 extracted from

  • Qian, X.; He, Y.; Wu, Y.; Luo, Y.
    Asp302 determines potassium dependence of a RadA recombinase from Methanococcus voltae (2006), J. Mol. Biol., 360, 537-547.
    View publication on PubMed
Search for more literature for 3.6.4.B7

Cloned(Commentary)

Cloned (Comment) Organism
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 Methanococcus voltae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop crystallization method at 21 °C. Enzyme in complex with AMP-PNP and K+ (2.7 A resolution), enzyme in complex with AMP-PNP (2.9 A resolution), enzyme in complex with ADP (2.4 A resolution) Methanococcus voltae

Protein Variants

Protein Variants Comment Organism
D302K mutant protein shows comparable strand exchange efficiencies in the presence of either potassium or sodium Methanococcus voltae
E151D mutant protein retains potassium preference in promoting strand exchange. Reduced ATPase activity and normal strand exchange activity Methanococcus voltae
E151K mutant protein retains potassium preference in promoting strand exchange. Reduced ATPase activity and normal strand exchange activity Methanococcus voltae

Inhibitors

Inhibitors Comment Organism Structure
NaCl minimal inhibitory effect by 40 mM NaCl further suggests that the protein does not have adequate affinity for sodium Methanococcus voltae

Metals/Ions

Metals/Ions Comment Organism Structure
K+ Mg2+ als well as K+ ions are absorbed at the ATPase center. K+ (but not Na+), stimulates the ATP hydrolysis reaction with an apparent dissociation constant of about 40 mM. The strand exchange activity of the wild-type enzyme is also stimulated by potassium with an apparent dissociation constant of 35 mM Methanococcus voltae
Mg2+ Mg2+ als well as K+ ions are absorbed at the ATPase center Methanococcus voltae

Organism

Organism UniProt Comment Textmining
Methanococcus voltae O73948
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O both ATP hydrolysis and DNA strand exchange requires accessibility to an active conformation similar to the crystallized ATPase-active form in the presence of ATP, Mg2+ and K+ Methanococcus voltae ADP + phosphate
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