1w78: Difference between revisions

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.

1W78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, SO4, PD8 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_synthase Dihydrofolate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.12 6.3.2.12] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W78 OCA].  

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