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Literature summary for 3.2.1.B28 extracted from

  • Nakabayashi, M.; Kataoka, M.; Watanabe, M.; Ishikawa, K.
    Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form (2014), Acta Crystallogr. Sect. F, 70, 854-859.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.B28

Cloned(Commentary)

Cloned (Comment) Organism
recombinant mutant that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449Kis expressed in Escherichia coli BL21 Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method, a monomeric form of the enzyme is constructed by removing the C-terminal region (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K) of the enzyme and its crystal structure is solved at a resolution of 2.8 A in space group Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
additional information a mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. The lack of the C-terminal region does not affect the activity of the enzyme, but disrupts its oligomeric state and hyperthermostability Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q51723
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Subunits

Subunits Comment Organism
dodecamer a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal Pyrococcus furiosus
monomer a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal Pyrococcus furiosus
tetramer the native enzyme forms a stable tetrameric structure Pyrococcus furiosus

Synonyms

Synonyms Comment Organism
BGLPf
-
 Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75 80 the mutant enzyme that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K is immediately inactivated between 75 and 80°C Pyrococcus furiosus
85
-
 wild-type enzyme is stable beyond 85°C Pyrococcus furiosus
110
-
 Tm-value of wild-type enzyme Pyrococcus furiosus