1w7k

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[[Image:1w7k.gif|left|200px]]
 
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{{Structure
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==E.coli FolC in complex with ADP, without folate substrate==
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|PDB= 1w7k |SIZE=350|CAPTION= <scene name='initialview01'>1w7k</scene>, resolution 2.1&Aring;
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<StructureSection load='1w7k' size='340' side='right'caption='[[1w7k]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=LCX:CARBOXYLATED+LYSINE'>LCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1w7k]] 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=1W7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7K FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1w7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7k OCA], [https://pdbe.org/1w7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7k RCSB], [https://www.ebi.ac.uk/pdbsum/1w7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7k ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7k OCA], [http://www.ebi.ac.uk/pdbsum/1w7k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w7k RCSB]</span>
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== Function ==
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}}
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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/w7/1w7k_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=1w7k 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 ADP, WITHOUT FOLATE SUBSTRATE'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1w7k" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]]
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== References ==
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==About this Structure==
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<references/>
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1W7K 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=1W7K OCA].
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__TOC__
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</StructureSection>
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==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://www.ncbi.nlm.nih.gov/pubmed/15705579 15705579]
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[[Category: Dihydrofolate synthase]]
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[[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 Mon Mar 31 00:32:18 2008''
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Current revision

E.coli FolC in complex with ADP, without folate substrate

PDB ID 1w7k

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