3L2I
1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2.
Summary for 3L2I
| Entry DOI | 10.2210/pdb3l2i/pdb |
| Descriptor | 3-dehydroquinate dehydratase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | 3-dehydroquinate dehydratase, arod, shikimate pathway, idp90922, csgid, amino-acid biosynthesis, aromatic amino acid biosynthesis, lyase, schiff base, structural genomics, center for structural genomics of infectious diseases |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 2 |
| Total formula weight | 60226.92 |
| Authors | Minasov, G.,Light, S.H.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2009-12-15, release date: 2009-12-29, Last modification date: 2023-09-06) |
| Primary citation | Light, S.H.,Minasov, G.,Shuvalova, L.,Peterson, S.N.,Caffrey, M.,Anderson, W.F.,Lavie, A. A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding. Biochemistry, 50:2357-2363, 2011 Cited by PubMed Abstract: Dehydroquinate dehydratase (DHQD) catalyzes the third step in the biosynthetic shikimate pathway. We present three crystal structures of the Salmonella enterica type I DHQD that address the functionality of a surface loop that is observed to close over the active site following substrate binding. Two wild-type structures with differing loop conformations and kinetic and structural studies of a mutant provide evidence of both direct and indirect mechanisms of involvement of the loop in substrate binding. In addition to allowing amino acid side chains to establish a direct interaction with the substrate, closure of the loop necessitates a conformational change of a key active site arginine, which in turn positions the substrate productively. The absence of DHQD in humans and its essentiality in many pathogenic bacteria make the enzyme a target for the development of nontoxic antimicrobials. The structures and ligand binding insights presented here may inform the design of novel type I DHQD inhibiting molecules. PubMed: 21291284DOI: 10.1021/bi102020s PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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