1w78

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[[Image:1w78.gif|left|200px]]<br /><applet load="1w78" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w78.gif|left|200px]]
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caption="1w78, resolution 1.82&Aring;" />
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'''E.COLI FOLC IN COMPLEX WITH DHPP AND ADP'''<br />
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{{Structure
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|PDB= 1w78 |SIZE=350|CAPTION= <scene name='initialview01'>1w78</scene>, resolution 1.82&Aring;
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|SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PD8:PHOSPHORYLATED+DIHYDROPTEROATE'>PD8</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''E.COLI FOLC IN COMPLEX WITH DHPP AND ADP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PD8:'>PD8</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W78 OCA].
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1W78 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W78 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15705579 15705579]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15705579 15705579]
[[Category: Dihydrofolate synthase]]
[[Category: Dihydrofolate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: SO4]]
[[Category: SO4]]
[[Category: atp-binding]]
[[Category: atp-binding]]
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[[Category: dhfs]]
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[[Category: dhf]]
[[Category: dihydrofolate synthase]]
[[Category: dihydrofolate synthase]]
[[Category: folate biosynthesis]]
[[Category: folate biosynthesis]]
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[[Category: synthase]]
[[Category: synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:07 2008''

Revision as of 12:53, 20 March 2008

Image:1w78.gif


PDB ID 1w78

Drag the structure with the mouse to rotate
, resolution 1.82Å
Sites:
Ligands: , , and
Activity: Dihydrofolate synthase, with EC number 6.3.2.12
Coordinates: save as pdb, mmCIF, xml



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. 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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