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Literature summary for 3.2.1.4 extracted from

  • Chang, C.J.; Lee, C.C.; Chan, Y.T.; Trudeau, D.L.; Wu, M.H.; Tsai, C.H.; Yu, S.M.; Ho, T.H.; Wang, A.H.; Hsiao, C.D.; Arnold, F.H.; Chao, Y.C.
    Exploring the mechanism responsible for cellulase thermostability by structure-guided recombination (2016), PLoS ONE, 11, e0147485.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.4

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of chimera C10 in complex with crown ether. The structure of C10 adopts the same classical TIM barrel fold as the parental structures of CelA core and Cel5A. A Ca2+ ion is bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A Geobacillus sp.
structure of chimera C10 in complex with crown ether. The structure of C10 adopts the same classical TIM barrel fold as the parental structures of CelA core and Cel5A. A Ca2+ ion is bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C Geobacillus sp.
additional information generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ chimeric construct C10 has a Ca2+ ion bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A Geobacillus sp.
Ca2+ chimeric construct C10 has a Ca2+ ion bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P10475
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Bacillus subtilis 168 P10475
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Geobacillus sp. C5H6X3
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Geobacillus sp. 70PC53 C5H6X3
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-

Synonyms

Synonyms Comment Organism
Cel5A
-
 Bacillus subtilis
EglS
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 Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
79
-
 wild-type, 10 min, 50% loss of activity Geobacillus sp.
79
-
 wild-type, 10 min, 50% loss of activity Bacillus subtilis
83
-
 chimeric construct C10, 10 min, 50% loss of activity Geobacillus sp.
83
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 chimeric construct C10, 10 min, 50% loss of activity Bacillus subtilis