1QFE
THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI
Summary for 1QFE
| Entry DOI | 10.2210/pdb1qfe/pdb |
| Descriptor | PROTEIN (3-DEHYDROQUINATE DEHYDRATASE), 3-AMINO-4,5-DIHYDROXY-CYCLOHEX-1-ENECARBOXYLATE (3 entities in total) |
| Functional Keywords | dehydratase, conversion of 3-dehydroquinate to dehydroshikimate, 3rd enzyme in the shikimate pathway, tim barrel, lyase |
| Biological source | Salmonella typhi |
| Total number of polymer chains | 2 |
| Total formula weight | 55654.14 |
| Authors | Shrive, A.K.,Polikarpov, I.,Sawyer, L.,Coggins, J.R.,Hawkins, A.R. (deposition date: 1999-04-05, release date: 2000-04-05, Last modification date: 2024-11-13) |
| Primary citation | Gourley, D.G.,Shrive, A.K.,Polikarpov, I.,Krell, T.,Coggins, J.R.,Hawkins, A.R.,Isaacs, N.W.,Sawyer, L. The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction. Nat.Struct.Biol., 6:521-525, 1999 Cited by PubMed Abstract: The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well conserved as are their catalytic mechanisms. The two types of 3-dehydroquinate dehydratase (DHQase) are therefore most unusual since they are unrelated at the sequence level and they utilize completely different mechanisms to catalyze the same overall reaction. The type I enzymes catalyze a cis-dehydration of 3-dehydroquinate via a covalent imine intermediate, while the type II enzymes catalyze a trans-dehydration via an enolate intermediate. Here we report the three-dimensional structures of a representative member of each type of biosynthetic DHQase. Both enzymes function as part of the shikimate pathway, which is essential in microorganisms and plants for the biosynthesis of aromatic compounds including folate, ubiquinone and the aromatic amino acids. An explanation for the presence of two different enzymes catalyzing the same reaction is presented. The absence of the shikimate pathway in animals makes it an attractive target for antimicrobial agents. The availability of these two structures opens the way for the design of highly specific enzyme inhibitors with potential importance as selective therapeutic agents. PubMed: 10360352DOI: 10.1038/9287 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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