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Literature summary for 3.6.4.13 extracted from

  • Leshchiner, A.D.; Solovyev, A.G.; Morozov, S.Y.; Kalinina, N.O.
    A minimal region in the NTPase/helicase domain of the TGBp1 plant virus movement protein is responsible for ATPase activity and cooperative RNA binding (2006), J. Gen. Virol., 87, 3087-3095.
    View publication on PubMed
Search for more literature for 3.6.4.13

Protein Variants

Protein Variants Comment Organism
additional information the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinĀ–protein interactions. Point mutations in a single conserved basic amino acid residue upstream of motif I have little effect on the activities of C-terminally truncated mutants of both TGBp1 proteins. When introduced into the full-length NTPase/helicase domains, these mutations cause a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I is required to maintain a reaction-competent conformation of the TGBp1 ATPase active site potato virus X
additional information the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinĀ–protein interactions. Point mutations in a single conserved basic amino acid residue upstream of motif I have little effect on the activities of C-terminally truncated mutants of both TGBp1 proteins. When introduced into the full-length NTPase/helicase domains, these mutations cause a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I is required to maintain a reaction-competent conformation of the TGBp1 ATPase active site Poa semilatent virus

Organism

Organism UniProt Comment Textmining
Poa semilatent virus
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potato virus X
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinĀ–protein interactions potato virus X ADP + phosphate
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 ?
ATP + H2O the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinĀ–protein interactions Poa semilatent virus ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
TGBp1 NTPase/helicase domain
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 potato virus X
TGBp1 NTPase/helicase domain
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 Poa semilatent virus