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Structure paper

TitleConformational Tinkering Drives Evolution of a Promiscuous Activity through Indirect Mutational Effects.
Journal, issue, pagesBiochemistry, Vol. 55, Page 4583-4593, Year 2016
Publish dateOct 28, 2015 (structure data deposition date)
AuthorsYang, G. / Hong, N. / Baier, F. / Jackson, C.J. / Tokuriki, N.
External linksBiochemistry / PubMed:27444875
MethodsX-ray diffraction
Resolution1.29 Å
Structure data

PDB-5eh9:
Indirect contributions of mutations underlie optimization of new enzyme function
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

PDB-5eht:
Indirect contributions of mutations underlie optimization of new enzyme function
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HED:
2-HYDROXYETHYL DISULFIDE

ChemComp-HOH:
WATER

Source
  • bacillus thuringiensis subsp. kurstaki (bacteria)
  • bacillus thuringiensis (bacteria)
KeywordsHYDROLASE / N-Acyl homoserine lactonase from Bacillus thuringiensis / N-Acyl-Homoserine Lactonase / Directed evolution / AiiA / QQL / Lactonase / Phosphatase / Paraoxonase

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