1NPY
Structure of shikimate 5-dehydrogenase-like protein HI0607
Summary for 1NPY
| Entry DOI | 10.2210/pdb1npy/pdb |
| Descriptor | Hypothetical shikimate 5-dehydrogenase-like protein HI0607, ACETYL GROUP (3 entities in total) |
| Functional Keywords | structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 4 |
| Total formula weight | 119997.90 |
| Authors | Korolev, S.,Koroleva, O.,Zarembinski, T.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2003-01-20, release date: 2003-07-29, Last modification date: 2024-02-14) |
| Primary citation | Singh, S.,Korolev, S.,Koroleva, O.,Zarembinski, T.,Collart, F.,Joachimiak, A.,Christendat, D. Crystal Structure of a Novel Shikimate Dehydrogenase from Haemophilus influenzae. J.Biol.Chem., 280:17101-17108, 2005 Cited by PubMed Abstract: To date two classes of shikimate dehydrogenases have been identified and characterized, YdiB and AroE. YdiB is a bifunctional enzyme that catalyzes the reversible reductions of dehydroquinate to quinate and dehydroshikimate to shikimate in the presence of either NADH or NADPH. In contrast, AroE catalyzes the reversible reduction of dehydroshikimate to shikimate in the presence of NADPH. Here we report the crystal structure and biochemical characterization of HI0607, a novel class of shikimate dehydrogenase annotated as shikimate dehydrogenase-like. The kinetic properties of HI0607 are remarkably different from those of AroE and YdiB. In comparison with YdiB, HI0607 catalyzes the oxidation of shikimate but not quinate. The turnover rate for the oxidation of shikimate is approximately 1000-fold lower compared with that of AroE. Phylogenetic analysis reveals three independent clusters representing three classes of shikimate dehydrogenases, namely AroE, YdiB, and this newly characterized shikimate dehydrogenase-like protein. In addition, mutagenesis studies of two invariant residues, Asp-103 and Lys-67, indicate that they are important catalytic groups that may function as a catalytic pair in the shikimate dehydrogenase reaction. This is the first study that describes the crystal structure as well as mutagenesis and mechanistic analysis of this new class of shikimate dehydrogenase. PubMed: 15735308DOI: 10.1074/jbc.M412753200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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