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

Authors: Maes, D.; Gonzalez-Ramirez, L. A.; Lopez-Jaramillo, J.; Yu, B.; De Bondt, H.; Zegers, I.; Afonina, E.; Garcia-Ruiz, J. M.; Gulnik, S.

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 463-471(9)

Publisher: Blackwell Publishing

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

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 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.

Keywords: 3-dehydroquinate dehydratase

Document Type: Research article

DOI: 10.1107/S090744490302969X

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.16 plus tax Refund Policy