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EC Number	Crystallization (Commentary)
3.5.1.97	1.8 A resolution. PvdQ has a typical alpha/beta heterodimeric Ntn-hydrolase fold. It has a large, hydrophobic binding pocket, ideally suited to recognize C12 fatty acid-like chains of N-acylhomoserine lactones. Binding of a C12 fatty acid or a 3-oxo-C12 fatty acid induces subtle conformational changes to accommodate the aliphatic chain. PvdQ is the first structurally characterized Ntn-hydrolase within this family to have any disulfide bridges. The disulfides are located in both the alpha- and beta-chain on the periphery of the protein

EC Number

Crystallization (Commentary)

3.5.1.97

1.8 A resolution. PvdQ has a typical alpha/beta heterodimeric Ntn-hydrolase fold. It has a large, hydrophobic binding pocket, ideally suited to recognize C12 fatty acid-like chains of N-acylhomoserine lactones. Binding of a C12 fatty acid or a 3-oxo-C12 fatty acid induces subtle conformational changes to accommodate the aliphatic chain. PvdQ is the first structurally characterized Ntn-hydrolase within this family to have any disulfide bridges. The disulfides are located in both the alpha- and beta-chain on the periphery of the protein

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Release 2023.1 (January 2023)