1w78

From Proteopedia

Revision as of 14:22, 30 October 2007

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 ... [(full description)]

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]. Structure known Active Site: AC1. 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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