3OEX
Crystal Structure of Type I 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium with close loop conformation.
Summary for 3OEX
| Entry DOI | 10.2210/pdb3oex/pdb |
| Related | 3L2I 3LB0 3M7W 3NNT 3O1N |
| Descriptor | 3-dehydroquinate dehydratase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, tim barrel, lyase |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 4 |
| Total formula weight | 110660.42 |
| Authors | Minasov, G.,Light, S.H.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2010-08-13, release date: 2010-09-01, 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 (1.9 Å) |
Structure validation
Download full validation report
