1w78

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[[Image:1w78.gif|left|200px]]<br /><applet load="1w78" size="450" color="white" frame="true" align="right" spinBox="true"
 
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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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==Overview==
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==E.coli FolC in complex with DHPP and ADP==
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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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<StructureSection load='1w78' size='340' side='right'caption='[[1w78]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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==About this Structure==
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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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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] Known structural/functional Site: <scene name='pdbsite=AC1:Adp Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W78 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Dihydrofolate synthase]]
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<div class="pdbe-citations 1w78" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Bamas-Jacques, N.]]
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[[Category: Debousker, G.]]
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[[Category: Mathieu, M.]]
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[[Category: Mikol, V.]]
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[[Category: Vincent, S.]]
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[[Category: Viviani, F.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: PD8]]
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[[Category: SO4]]
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[[Category: atp-binding]]
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[[Category: dhfs]]
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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://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:33:09 2007''
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==See Also==
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*[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Bamas-Jacques N]]
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[[Category: Debousker G]]
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[[Category: Mathieu M]]
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[[Category: Mikol V]]
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[[Category: Vincent S]]
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[[Category: Viviani F]]

Current revision

E.coli FolC in complex with DHPP and ADP

PDB ID 1w78

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