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PMID:9417939
| Citation |
Blickling, S, Beisel, HG, Bozic, D, Knäblein, J, Laber, B and Huber, R (1997) Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure. J. Mol. Biol. 274:608-21 |
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| Abstract |
DHDPS is the first enzyme unique to the lysine biosynthetic pathway in plants and bacteria and catalyses the formation of (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid. It is feedback-regulated in plants by L-lysine. The crystal structure of Nicotiana sylvestris DHDPS with and without inhibitory lysine bound to the enzyme has been solved to a resolution of 2.8 A. The molecule is a homotetramer composed of a dimer of dimers. Comparison with the structure of Escherichia coli DHDPS showed a novel quaternary structure by a profound rearrangement of the dimers forming the tetramer. The crystal structure of the enzyme in the presence of L-lysine revealed substantial changes. These changes together with the novel quaternary structure provide a structural basis for the strong inhibition of plant DHDPS enzymes by L-lysine. |
| Links |
PubMed Online version:10.1006/jmbi.1997.1393 |
| Keywords |
Amino Acid Sequence; Binding Sites; Conserved Sequence; Enzyme Inhibitors/chemistry; Enzyme Inhibitors/metabolism; Escherichia coli/enzymology; Hydro-Lyases/antagonists & inhibitors; Hydro-Lyases/chemistry; Hydro-Lyases/metabolism; Lysine/chemistry; Lysine/metabolism; Models, Molecular; Molecular Sequence Data; Plants, Toxic; Protein Conformation; Tobacco/enzymology |
| edit table |
Significance
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