1W7K
E.coli FolC in complex with ADP, without folate substrate
Summary for 1W7K
| Entry DOI | 10.2210/pdb1w7k/pdb |
| Related | 1W78 |
| Descriptor | FOLC BIFUNCTIONAL PROTEIN, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | folc, dhfs, dihydrofolate synthase, synthase, atp-binding, folate biosynthesis, ligase, multifunctional enzyme |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 46071.42 |
| Authors | Mathieu, M.,Debousker, G.,Vincent, S.,Viviani, F.,Bamas-Jacques, N.,Mikol, V. (deposition date: 2004-09-06, release date: 2005-02-09, Last modification date: 2023-12-13) |
| Primary citation | Mathieu, M.,Debousker, G.,Vincent, S.,Viviani, F.,Bamas-Jacques, N.,Mikol, V. Escherichia Coli Folc Structure Reveals an Unexpected Dihydrofolate Binding Site Providing an Attractive Target for Anti-Microbial Therapy J.Biol.Chem., 280:18916-, 2005 Cited by PubMed Abstract: In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (folylpolyglutamate synthetase (FPGS) activity) are catalyzed by the same enzyme, FolC. The crystal structure of E. coli FolC is described in this paper. It showed strong similarities to that of the FPGS enzyme of Lactobacillus casei within the ATP binding site and the catalytic site, as do all other members of the Mur synthethase superfamily. FolC structure revealed an unexpected dihydropteroate binding site very different from the folate site identified previously in the FPGS structure. The relevance of this site is exemplified by the presence of phosphorylated dihydropteroate, a reaction intermediate in the DHFS reaction. L. casei FPGS is considered a relevant model for human FPGS. As such, the presence of a folate binding site in E. coli FolC, which is different from the one seen in FPGS enzymes, provides avenues for the design of specific inhibitors of this enzyme in antimicrobial therapy. PubMed: 15705579DOI: 10.1074/JBC.M413799200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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