1w78: Difference between revisions
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<StructureSection load='1w78' size='340' side='right'caption='[[1w78]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='1w78' size='340' side='right'caption='[[1w78]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w78]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FOLC_ECOLI FOLC_ECOLI] Conversion of folates to polyglutamate derivatives. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bamas-Jacques | [[Category: Bamas-Jacques N]] | ||
[[Category: Debousker | [[Category: Debousker G]] | ||
[[Category: Mathieu | [[Category: Mathieu M]] | ||
[[Category: Mikol | [[Category: Mikol V]] | ||
[[Category: Vincent | [[Category: Vincent S]] | ||
[[Category: Viviani | [[Category: Viviani F]] | ||
Latest revision as of 16:19, 13 December 2023
E.coli FolC in complex with DHPP and ADPE.coli FolC in complex with DHPP and ADP
Structural highlights
FunctionFOLC_ECOLI Conversion of folates to polyglutamate derivatives. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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