1fgs: Difference between revisions
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<StructureSection load='1fgs' size='340' side='right' caption='[[1fgs]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1fgs' size='340' side='right' caption='[[1fgs]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fgs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1fgs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_a"_von_freudenreich_1890 "bacillus a" von freudenreich 1890]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tetrahydrofolate_synthase Tetrahydrofolate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.17 6.3.2.17] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tetrahydrofolate_synthase Tetrahydrofolate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.17 6.3.2.17] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgs RCSB], [http://www.ebi.ac.uk/pdbsum/1fgs PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgs OCA], [http://pdbe.org/1fgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgs RCSB], [http://www.ebi.ac.uk/pdbsum/1fgs PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1fgs" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus a von freudenreich 1890]] | ||
[[Category: Tetrahydrofolate synthase]] | [[Category: Tetrahydrofolate synthase]] | ||
[[Category: Baker, E]] | [[Category: Baker, E]] | ||
Revision as of 17:27, 11 September 2015
FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEIFOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI
Structural highlights
Function[FOLC_LACCA] Conversion of folates to polyglutamate derivatives. It prefers 5,10-methylenetetrahydrofolate, rather than 10-formyltetrahydrofolate as folate substrate. 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 PubMedFolylpolyglutamate synthetase, which is responsible for the addition of a polyglutamate tail to folate and folate derivatives, is an ATP-dependent enzyme isolated from eukaryotic and bacterial sources, where it plays a key role in the retention of the intracellular folate pool. Here, we report the 2.4-A resolution crystal structure of the MgATP complex of the enzyme from Lactobacillus casei. The structural analysis reveals that folylpolyglutamate synthetase is a modular protein consisting of two domains, one with a typical mononucleotide-binding fold and the other strikingly similar to the folate-binding enzyme dihydrofolate reductase. We have located the active site of the enzyme in a large interdomain cleft adjacent to an ATP-binding P-loop motif. Opposite this site, in the C domain, a cavity likely to be the folate binding site has been identified, and inspection of this cavity and the surrounding protein structure suggests that the glutamate tail of the substrate may project into the active site. A further feature of the structure is a well defined Omega loop, which contributes both to the active site and to interdomain interactions. The determination of the structure of this enzyme represents the first step toward the elucidation of the molecular mechanism of polyglutamylation of folates and antifolates. Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase.,Sun X, Bognar AL, Baker EN, Smith CA Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6647-52. PMID:9618466[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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