1W78

E.coli FolC in complex with DHPP and ADP

1W78 の概要

• エントリーDOI: 10.2210/pdb1w78/pdb
• 関連するPDBエントリー: 1W7K
• 分子名称: FOLC BIFUNCTIONAL PROTEIN, PHOSPHORYLATED DIHYDROPTEROATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: folc, dhfs, dihydrofolate synthase, synthase, atp-binding, folate biosynthesis, ligase, multifunctional enzyme
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46463.68

構造登録者

Mathieu, M.,Debousker, G.,Vincent, S.,Viviani, F.,Bamas-Jacques, N.,Mikol, V. (登録日: 2004-08-31, 公開日: 2005-02-09, 最終更新日: 2023-12-13)

主引用文献

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

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: 15705579
DOI: 10.1074/JBC.M413799200

実験手法

X-RAY DIFFRACTION (1.82 Å)