2F1K

Crystal structure of Synechocystis arogenate dehydrogenase

Summary for 2F1K

• Entry DOI: 10.2210/pdb2f1k/pdb
• Descriptor: prephenate dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: arogenate/prephenate dehydrogenase, tyrosine synthesis, x-ray crystallography structure, oxidoreductase
• Biological source: Synechocystis sp.
• Total number of polymer chains: 4
• Total formula weight: 124516.35

Authors

Legrand, P.,Dumas, R.,Seux, M.,Rippert, P.,Ravelli, R.,Ferrer, J.-L.,Matringe, M. (deposition date: 2005-11-14, release date: 2006-05-09, Last modification date: 2025-03-26)

Primary citation

Legrand, P.,Dumas, R.,Seux, M.,Rippert, P.,Ravelli, R.,Ferrer, J.-L.,Matringe, M.
Biochemical Characterization and Crystal Structure of Synechocystis Arogenate Dehydrogenase Provide Insights into Catalytic Reaction
Structure, 14:767-776, 2006

PubMed Abstract: The extreme diversity in substrate specificity, and in the regulation mechanism of arogenate/prephenate dehydrogenase enzymes in nature, makes a comparative structural study of these enzymes of great interest. We report here on the biochemical and structural characterization of arogenate dehydrogenase from Synechocystis sp. (TyrAsy). This work paves the way for the understanding of the structural determinants leading to diversity in substrate specificity, and of the regulation mechanisms of arogenate/prephenate dehydrogenases. The overall structure of TyrAsy in complex with NADP was refined to 1.6 A. The asymmetric unit contains two TyrAsy homodimers, with each monomer consisting of a nucleotide binding N-terminal domain and a particularly unique alpha-helical C-terminal dimerization domain. The substrate arogenate was modeled into the active site. The model of the ternary complex enzyme-NADP-arogenate nicely reveals at the atomic level the concerted mechanism of the arogenate/prephenate dehydrogenase reaction.

PubMed: 16615917
DOI: 10.1016/j.str.2006.01.006

Experimental method

X-RAY DIFFRACTION (1.55 Å)