2g5c | pdb_00002g5c

Crystal Structure of Prephenate Dehydrogenase from Aquifex aeolicus

spinqualitylabelsall models 2g5c, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2g5c is a 4 chain structure with sequence from Aquae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAD NonStd Res: MSE Activity: Prephenate dehydrogenase, with EC number 1.3.1.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The enzyme prephenate dehydrogenase catalyzes the oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate for the biosynthesis of tyrosine. Prephenate dehydrogenases exist as either monofunctional or bifunctional enzymes. The bifunctional enzymes are diverse, since the prephenate dehydrogenase domain is associated with other enzymes, such as chorismate mutase and 3-phosphoskimate 1-carboxyvinyltransferase. We report the first crystal structure of a monofunctional prephenate dehydrogenase enzyme from the hyper-thermophile Aquifex aeolicus in complex with NAD+. This protein consists of two structural domains, a modified nucleotide-binding domain and a novel helical prephenate binding domain. The active site of prephenate dehydrogenase is formed at the domain interface and is shared between the subunits of the dimer. We infer from the structure that access to the active site is regulated via a gated mechanism, which is modulated by an ionic network involving a conserved arginine, Arg250. In addition, the crystal structure reveals for the first time the positions of a number of key catalytic residues and the identity of other active site residues that may participate in the reaction mechanism; these residues include Ser126 and Lys246 and the catalytic histidine, His147. Analysis of the structure further reveals that two secondary structure elements, beta3 and beta7, are missing in the prephenate dehydrogenase domain of the bifunctional chorismate mutase-prephenate dehydrogenase enzymes. This observation suggests that the two functional domains of chorismate mutase-prephenate dehydrogenase are interdependent and explains why these domains cannot be separated. Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism.,Sun W, Singh S, Zhang R, Turnbull JL, Christendat D J Biol Chem. 2006 May 5;281(18):12919-28. Epub 2006 Mar 2. PMID:16513644 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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