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TitleMechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
Journal, issue, pagesBiochemistry, Vol. 47, Page 7706-7714, Year 2008
Publish dateJun 17, 2008 (structure data deposition date)
AuthorsLiu, D. / Momb, J. / Thomas, P.W. / Moulin, A. / Petsko, G.A. / Fast, W. / Ringe, D.
External linksBiochemistry / PubMed:18627129
MethodsX-ray diffraction
Resolution0.95 - 1.4 Å
Structure data

PDB-3dha:
An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site
Method: X-RAY DIFFRACTION / Resolution: 0.95 Å

PDB-3dhb:
1.4 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at The Catalytic Metal Center
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3dhc:
1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homocysteine Bound to The catalytic Metal Center
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-C6L:
N-hexanoyl-L-homoserine

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CYK:
N-hexanoyl-L-homocysteine

Source
  • bacillus thuringiensis serovar kurstaki (bacteria)
KeywordsHYDROLASE / Zinc Bimetallohydrolase / Quorum Quenching / N-Acyl Homoserine lactone / Alternative Binding Site / Product Complex / AHL Lactonase / Qourum Quenching / General Acid / Catalytic Mechanism / N-Acyl Homocysteine Thiolactone

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