1w78

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[[Image:1w78.gif|left|200px]]
 
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==E.coli FolC in complex with DHPP and ADP==
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The line below this paragraph, containing "STRUCTURE_1w78", creates the "Structure Box" on the page.
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<StructureSection load='1w78' size='340' side='right'caption='[[1w78]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w78]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W78 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PD8:PHOSPHORYLATED+DIHYDROPTEROATE'>PD8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1w78| PDB=1w78 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w78 OCA], [https://pdbe.org/1w78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w78 RCSB], [https://www.ebi.ac.uk/pdbsum/1w78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w78 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FOLC_ECOLI FOLC_ECOLI] Conversion of folates to polyglutamate derivatives.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/1w78_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w78 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''E.COLI FOLC IN COMPLEX WITH DHPP AND ADP'''
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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:15705579<ref>PMID:15705579</ref>
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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].
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</div>
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<div class="pdbe-citations 1w78" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]]
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[[Category: Dihydrofolate synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bamas-Jacques, N.]]
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[[Category: Bamas-Jacques N]]
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[[Category: Debousker, G.]]
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[[Category: Debousker G]]
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[[Category: Mathieu, M.]]
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[[Category: Mathieu M]]
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[[Category: Mikol, V.]]
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[[Category: Mikol V]]
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[[Category: Vincent, S.]]
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[[Category: Vincent S]]
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[[Category: Viviani, F.]]
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[[Category: Viviani F]]
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[[Category: Atp-binding]]
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[[Category: Dhf]]
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[[Category: Dihydrofolate synthase]]
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[[Category: Folate biosynthesis]]
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[[Category: Folc]]
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[[Category: Ligase]]
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[[Category: Multifunctional enzyme]]
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[[Category: Synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:15:09 2008''
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Current revision

E.coli FolC in complex with DHPP and ADP

PDB ID 1w78

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