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Structure paper

TitleStructural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.
Journal, issue, pagesSci Rep, Vol. 8, Page 11262-11262, Year 2018
Publish dateFeb 21, 2018 (structure data deposition date)
AuthorsBergonzi, C. / Schwab, M. / Naik, T. / Daude, D. / Chabriere, E. / Elias, M.
External linksSci Rep / PubMed:30050039
MethodsX-ray diffraction
Resolution1.65 - 2.15 Å
Structure data

PDB-6cgy:
Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound to a phosphate anion
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6cgz:
Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound to C6-AHL
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6ch0:
Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound to a glycerol molecule
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-CO:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-HL6:
N-[(3S)-2-oxotetrahydrofuran-3-yl]hexanamide

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

Source
  • alicyclobacillus acidoterrestris (strain atcc 49025 / dsm 3922 / cip 106132 / ncimb 13137 / gd3b) (bacteria)
KeywordsHYDROLASE / lactonase / acyl homoserine lactone hydrolase

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