4L8L
Crystal Structure of the Type II Dehydroquinase from Pseudomonas aeruginosa
Summary for 4L8L
| Entry DOI | 10.2210/pdb4l8l/pdb |
| Descriptor | 3-dehydroquinate dehydratase 1 (2 entities in total) |
| Functional Keywords | flavodoxin-like fold, rossmann fold, alpha helix, beta sheet, dehydratase, dehydroquinic acid, lyase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 15985.02 |
| Authors | Reiling, S.A.,Asojo, O.A. (deposition date: 2013-06-17, release date: 2014-07-23, Last modification date: 2024-02-28) |
| Primary citation | Reiling, S.,Kelleher, A.,Matsumoto, M.M.,Robinson, G.,Asojo, O.A. Structure of type II dehydroquinase from Pseudomonas aeruginosa. Acta Crystallogr F Struct Biol Commun, 70:1485-1491, 2014 Cited by PubMed Abstract: Pseudomonas aeruginosa causes opportunistic infections and is resistant to most antibiotics. Ongoing efforts to generate much-needed new antibiotics include targeting enzymes that are vital for P. aeruginosa but are absent in mammals. One such enzyme, type II dehydroquinase (DHQase), catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate, a necessary step in the shikimate pathway. This step is vital for the proper synthesis of phenylalanine, tryptophan, tyrosine and other aromatic metabolites. The recombinant expression, purification and crystal structure of catalytically active DHQase from P. aeruginosa (PaDHQase) are presented. Cubic crystals belonging to space group F23, with unit-cell parameters a=b=c=125.39 Å, were obtained by vapor diffusion in sitting drops and the structure was refined to an R factor of 16% at 1.74 Å resolution. PaDHQase is a prototypical type II DHQase with the classical flavodoxin-like α/β topology. PubMed: 25372814DOI: 10.1107/S2053230X14020214 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
Download full validation report
