Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.
作者： D. Maes , L. A. Gonzalez-Ramirez , J. Lopez-Jaramillo , B. Yu , H. De Bondt
DOI: 10.1107/S090744490302969X
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摘要: The structure of the type II dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae, third enzyme shikimate pathway, has been determined. Crystals diffracting to 1.7 A were obtained in space and on earth using counter-diffusion technique. was solved molecular replacement refined high resolution. overall dodecameric is described compared with structures DHQases other bacteria. contain a flexible loop that presumably closes over active site upon substrate binding. can exist an open or closed conformation. present displays conformation, sulfate anion bound site. availability this opens route structure-based antibiotics targetting pathogenic bacterium.
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