1UQR

Type II 3-dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae

Summary for 1UQR

• Entry DOI: 10.2210/pdb1uqr/pdb
• Descriptor: 3-DEHYDROQUINATE DEHYDRATASE, SULFATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: shikimate pathway, aromatic amino acid biosynthesis, lyase
• Biological source: ACTINOBACILLUS PLEUROPNEUMONIAE
• Total number of polymer chains: 12
• Total formula weight: 209836.38

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. (deposition date: 2003-10-16, release date: 2003-10-30, Last modification date: 2024-05-08)

Primary citation

Maes, D.,Gonzalez-Ramirez, L.A.,Lopez-Jaramillo, J.,Yu, B.,De Bondt, H.,Zegers, I.,Afonina, E.,Garcia-Ruiz, J.M.,Gulnik, S.
Structural Study of the Type II 3-Dehydroquinate Dehydratase from Actinobacillus Pleuropneumoniae
Acta Crystallogr.,Sect.D, 60:463-, 2004

PubMed 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 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.

PubMed: 14993670
DOI: 10.1107/S090744490302969X

Experimental method

X-RAY DIFFRACTION (1.7 Å)