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TitleStructure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.
Journal, issue, pagesOpen Biology, Vol. 11, Page 210182-210182, Year 2021
Publish dateDec 2, 2020 (structure data deposition date)
AuthorsNoby, N. / Auhim, H.S. / Winter, S. / Worthy, H.L. / Embaby, A.M. / Saeed, H. / Hussein, A. / Pudney, C.R. / Rizkallah, P.J. / Wells, S.A. / Jones, D.D.
External linksOpen Biology / PubMed:34847772
MethodsX-ray diffraction
Resolution1.61 Å
Structure data

PDB-7b4q:
Structure of a cold active HSL family esterase reveals mechanisms of low temperature adaptation and substrate specificity
Method: X-RAY DIFFRACTION / Resolution: 1.61 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bacillus cohnii nbrc 15565 (bacteria)
KeywordsHYDROLASE / Bacillus cohnii / esterase / low temperature adapted / regio-selective esterase / Hormone-sensitive family / lipase

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