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Structure paper

TitleA single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida.
Journal, issue, pagesCurr Res Biotechnol, Vol. 5, Year 2023
Publish dateFeb 24, 2023 (structure data deposition date)
AuthorsKuroki, C. / Hirano, Y. / Nakazawa, M. / Sakamoto, T. / Tamada, T. / Ueda, M.
External linksCurr Res Biotechnol / Search PubMed
MethodsX-ray diffraction
Resolution1.6 - 1.7 Å
Structure data

PDB-8ihw:
X-ray crystal structure of D43R mutant of endo-1,4-beta glucanase from Eisenia fetida
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-8ihx:
X-ray crystal structure of N372D mutant of endo-1,4-beta glucanase from Eisenia fetida
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-8ihy:
X-ray crystal structure of Q387E mutant of endo-1,4-beta glucanase from Eisenia fetida
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • eisenia fetida (common brandling worm)
KeywordsHYDROLASE / earthworm / cellulase / cold-adapted enzyme

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