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Structure paper

TitleStructural basis of mutants of PET-degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability.
Journal, issue, pagesProteins, Vol. 89, Page 502-511, Year 2021
Publish dateAug 20, 2020 (structure data deposition date)
AuthorsEmori, M. / Numoto, N. / Senga, A. / Bekker, G.J. / Kamiya, N. / Kobayashi, Y. / Ito, N. / Kawai, F. / Oda, M.
External linksProteins / PubMed:33340163
MethodsX-ray diffraction
Resolution1.1 - 1.2 Å
Structure data

PDB-7ctr:
Closed form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-7cts:
Open 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: 1.1 Å

Chemicals

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

ChemComp-HOH:
WATER

ChemComp-BCN:
BICINE / pH buffer*YM

ChemComp-CA:
Unknown entry

Source
  • saccharomonospora viridis (bacteria)
KeywordsHYDROLASE / PROTEIN ENGINEERING / POLYESTERASE / disulfide bond / metal binding

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