1O9B
QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH
Summary for 1O9B
| Entry DOI | 10.2210/pdb1o9b/pdb |
| Descriptor | HYPOTHETICAL SHIKIMATE 5-DEHYDROGENASE-LIKE PROTEIN YDIB, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, quinate, shikimate, nad, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 2 |
| Total formula weight | 65352.89 |
| Authors | Michel, G.,Cygler, M. (deposition date: 2002-12-12, release date: 2003-02-01, Last modification date: 2024-10-23) |
| Primary citation | Michel, G.,Roszak, A.W.,Sauve, V.,Mclean, J.,Matte, A.,Coggins, J.R.,Cygler, M.,Lapthorn, A.J. Structures of Shikimate Dehydrogenase Aroe and its Paralog Ydib: A Common Structural Framework for Different Activities J.Biol.Chem., 278:19463-, 2003 Cited by PubMed Abstract: Shikimate dehydrogenase catalyzes the fourth step of the shikimate pathway, the essential route for the biosynthesis of aromatic compounds in plants and microorganisms. Absent in metazoans, this pathway is an attractive target for nontoxic herbicides and drugs. Escherichia coli expresses two shikimate dehydrogenase paralogs, the NADP-specific AroE and a putative enzyme YdiB. Here we characterize YdiB as a dual specificity quinate/shikimate dehydrogenase that utilizes either NAD or NADP as a cofactor. Structures of AroE and YdiB with bound cofactors were determined at 1.5 and 2.5 A resolution, respectively. Both enzymes display a similar architecture with two alpha/beta domains separated by a wide cleft. Comparison of their dinucleotide-binding domains reveals the molecular basis for cofactor specificity. Independent molecules display conformational flexibility suggesting that a switch between open and closed conformations occurs upon substrate binding. Sequence analysis and structural comparison led us to propose the catalytic machinery and a model for 3-dehydroshikimate recognition. Furthermore, we discuss the evolutionary and metabolic implications of the presence of two shikimate dehydrogenases in E. coli and other organisms. PubMed: 12637497DOI: 10.1074/JBC.M300794200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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