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| {{STRUCTURE_1w78| PDB=1w78 | SCENE= }} | | {{STRUCTURE_1w78| PDB=1w78 | SCENE= }} |
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| '''E.COLI FOLC IN COMPLEX WITH DHPP AND ADP'''
| | ===E.COLI FOLC IN COMPLEX WITH DHPP AND ADP=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15705579}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15705579 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15705579}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Multifunctional enzyme]] | | [[Category: Multifunctional enzyme]] |
| [[Category: Synthase]] | | [[Category: Synthase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:15:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:29:14 2008'' |
