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Literature summary for 3.1.31.1 extracted from

  • Kitahara, R.; Hata, K.; Maeno, A.; Akasaka, K.; Chimenti, M.; Garcia-Moreno, E.; Schroer, M.; Jeworrek, C.; Tolan, M.; Winter, R.; Roche, J.; Roumestand, C.; Montet de Guillen, K.; Royer, C.
    Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH (2011), Proteins, 79, 1293-1305.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes in Escherichia coli Staphylococcus sp.

Protein Variants

Protein Variants Comment Organism
V66K the substitution affects the H/D exchange properties of the protein globally, even when Lys66 is neutral. The conformational dynamics of the protein probed by H/D exchange indicate that, while both the global fluctuation and the local fluctuation are increased by the substitution, the global fluctuations are enhanced by protonation of Lys-66 Staphylococcus sp.

Organism

Organism UniProt Comment Textmining
Staphylococcus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Staphylococcus sp.

Synonyms

Synonyms Comment Organism
SNase
-
Staphylococcus sp.
staphylococcal nuclease
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Staphylococcus sp.

General Information

General Information Comment Organism
physiological function presence and ionization of Lys66, buried in the hydrophobic core of a stabilized variant of staphylococcal nuclease, affect conformation and dynamics. The neutral Lys66 affects slow conformational fluctuations globally, whereas the effects of the charged form are localized to the region immediately surrounding position 66, when Lys66 is charged the protein expands, structural reorganization triggered by ionization of the internal Lys66, detailed overview Staphylococcus sp.