4B4U
Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor
Summary for 4B4U
| Entry DOI | 10.2210/pdb4b4u/pdb |
| Related | 4B4V 4B4W |
| Descriptor | BIFUNCTIONAL PROTEIN FOLD, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | ACINETOBACTER BAUMANNII ATCC 19606 |
| Total number of polymer chains | 2 |
| Total formula weight | 66372.55 |
| Authors | Eadsforth, T.C.,Maluf, F.V.,Hunter, W.N. (deposition date: 2012-08-01, release date: 2012-08-22, Last modification date: 2023-12-20) |
| Primary citation | Eadsforth, T.C.,Maluf, F.V.,Hunter, W.N. Acinetobacter Baumannii Fold Ligand Complexes; Potent Inhibitors of Folate Metabolism and a Re-Evaluation of the Ly374571 Structure. FEBS J., 279:4350-, 2012 Cited by PubMed Abstract: The bifunctional N(5),N(10)-methylenetetrahydrofolate dehydrogenase/cyclohydrolase (DHCH or FolD), which is widely distributed in prokaryotes and eukaryotes, is involved in the biosynthesis of folate cofactors that are essential for growth and cellular development. The enzyme activities represent a potential antimicrobial drug target. We have characterized the kinetic properties of FolD from the Gram-negative pathogen Acinetobacter baumanni and determined high-resolution crystal structures of complexes with a cofactor and two potent inhibitors. The data reveal new details with respect to the molecular basis of catalysis and potent inhibition. A unexpected finding was that our crystallographic data revealed a different structure for LY374571 (an inhibitor studied as an antifolate) than that previously published. The implications of this observation are discussed. PubMed: 23050773DOI: 10.1111/FEBS.12025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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