title: Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action.
abstract: Structural analyses of enzymes involved in biosynthetic pathways that are present in micro-organisms, but absent from mammals (for example Shikimate pathway) are important in developing anti-microbial drugs. Crystal structure of the Shikimate pathway enzyme, type I 3-dehydroquinate dehydratase (3-DHQase) from the hyperthermophilic bacterium Aquifex aeolicus was solved both as an apo form and in complex with a ligand. The complex structure revealed an interesting structural difference when compared to other ligand-bound type I 3-DHQases suggesting that closure of the active site loop is not essential for catalysis. This provides new insights into the catalytic mechanism of type I 3-DHQases.
authors: Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India.
authors: Aribam Swarmistha
authors: AS
authors: Devi
authors: Akio
authors: A
authors: Ebihara
authors: Seiki
authors: S
authors: Kuramitsu
authors: Shigeyuki
authors: S
authors: Yokoyama
authors: Thirumananseri
authors: T
authors: Kumarevel
authors: Karthe
authors: K
authors: Ponnuraj
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase