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Título

Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae

AutorMaes, D.; González-Ramírez, L. A.; López-Jaramillo, F. J.; Yu, B.; Bondt, H. de; Zegers, I.; Afonina, E.; García Ruiz, Juan Manuel; Gulnik, S.
Palabras clave3-dehydroquinate dehydratase
Fecha de publicaciónmar-2004
EditorInternational Union of Crystallography
CitaciónActa Crystallographica Section d Biological Crystallography 60(3): 463-471 (2004)
ResumenThe 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 Å 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.
Descripción9 pages, 7 figures, 2 tables.
Versión del editorhttp://dx.doi.org/10.1107/S090744490302969X
URIhttp://hdl.handle.net/10261/18858
DOI10.1107/S090744490302969X
ISSN0907-4449
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