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EC Number	Crystallization (Commentary)
2.3.1.262	crystal structures of the enzyme including the PqsD-anthranilate covalent intermediate and the inactive Cys112Ala active site mutant in complex with anthranilate. The crystallographic asymmetric unit contains a PqsD dimer. The PqsD monomer is composed of two nearly identical about 170 residue alphabetalaphabeta domains. Anthranilate-liganded residue Cys112 is positioned deep in the protein interior at the bottom of a 15 A long channel while a second anthraniloyl-CoA molecule is waiting in the cleft leading to the protein surface. Cys112, His257, and Asn287 form the FabH-like catalytic triad of PqsD
2.3.1.262	molecular dynamics simulations reveal a nucleophilic attack of the deprotonated sulfur of residue Cys112 at the carbonyl carbon of anthraniloyl-coenzyme A and a switch in the protonation pattern of His257 whereby Ndelta is protonated and the proton of Nepsilon? is shifted to the sulfur of CoA during the reaction

EC Number

Crystallization (Commentary)

2.3.1.262

crystal structures of the enzyme including the PqsD-anthranilate covalent intermediate and the inactive Cys112Ala active site mutant in complex with anthranilate. The crystallographic asymmetric unit contains a PqsD dimer. The PqsD monomer is composed of two nearly identical about 170 residue alphabetalaphabeta domains. Anthranilate-liganded residue Cys112 is positioned deep in the protein interior at the bottom of a 15 A long channel while a second anthraniloyl-CoA molecule is waiting in the cleft leading to the protein surface. Cys112, His257, and Asn287 form the FabH-like catalytic triad of PqsD

2.3.1.262

molecular dynamics simulations reveal a nucleophilic attack of the deprotonated sulfur of residue Cys112 at the carbonyl carbon of anthraniloyl-coenzyme A and a switch in the protonation pattern of His257 whereby Ndelta is protonated and the proton of Nepsilon? is shifted to the sulfur of CoA during the reaction

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Release 2023.1 (January 2023)