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Structure paper

TitleImprovement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism.
Journal, issue, pagesBiorxiv, Year 2023
Publish dateFeb 10, 2023 (structure data deposition date)
AuthorsNumoto, N. / Kamiya, N. / Oda, M.
External linksBiorxiv / Search PubMed
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-8ibl:
MES bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-8ibm:
Sulfate bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • saccharomonospora viridis (bacteria)
KeywordsHYDROLASE / PROTEIN ENGINEERING / POLYESTERASE / DISULFIDE BOND / METAL BINDING / Ligand complex

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