1uqr
From Proteopedia
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TYPE II 3-DEHYDROQUINATE DEHYDRATASE (DHQASE) FROM ACTINOBACILLUS PLEUROPNEUMONIAE
Overview
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.
About this Structure
1UQR is a Single protein structure of sequence from Actinobacillus pleuropneumoniae with SO4 and TRS as ligands. Active as 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae., Maes D, Gonzalez-Ramirez LA, Lopez-Jaramillo J, Yu B, De Bondt H, Zegers I, Afonina E, Garcia-Ruiz JM, Gulnik S, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):463-71. Epub 2004, Feb 25. PMID:14993670
Page seeded by OCA on Tue Dec 18 18:07:19 2007
Categories: 3-dehydroquinate dehydratase | Actinobacillus pleuropneumoniae | Single protein | Afonina, E. | Bondt, H.De. | Garcia-Ruiz, J.M. | Gonzalez-Ramirez, L.A. | Gulnik, S. | Lopez-Jaramillo, J. | Maes, D. | Yu, B. | Zegers, I. | SO4 | TRS | Aromatic amino acid biosynthesis | Lyase | Shikimate pathway
