Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.
The structure of the type II dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae, the third enzyme of the shikimate pathway, has been determined. Crystals diffracting to 1.7 A were obtained in space and on earth using the counter-diffusion technique. The structure was solved using molecular replacement and refined to high resolution. The overall structure of the dodecameric enzyme is described and compared with structures of DHQases from other bacteria. DHQases contain a flexible loop that presumably closes over the active site upon substrate binding. The enzyme can exist in an open or closed conformation. The present structure displays the open conformation, with a sulfate anion bound in the active site. The availability of this structure opens a route to structure-based antibiotics targetting this pathogenic bacterium.
ULTR, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Pleinlaan 2, 1050 Brussels, Belgium. dominique.maes@vub.ac.be
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D
Maes
L A
LA
Gonzalez-Ramirez
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J
Lopez-Jaramillo
B
B
Yu
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H
De Bondt
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I
Zegers
E
E
Afonina
J M
JM
Garcia-Ruiz
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Gulnik
D016977:Actinobacillus pleuropneumoniae / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D006836:Hydro-Lyases / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment
D001426:Bacterial Proteins; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase