1w78

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spinqualitylabelsall models 1w78, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

E.COLI FOLC IN COMPLEX WITH DHPP AND ADP

Overview

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.

About this Structure

1W78 is a Single protein structure of sequence from Escherichia coli with MG, SO4, PD8 and ADP as ligands. Active as Dihydrofolate synthase, with EC number 6.3.2.12 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy., Mathieu M, Debousker G, Vincent S, Viviani F, Bamas-Jacques N, Mikol V, J Biol Chem. 2005 May 13;280(19):18916-22. Epub 2005 Feb 10. PMID:15705579

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