1fgs: Difference between revisions

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-[[Image:1fgs.gif|left|200px]]<br /><applet load="1fgs" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fgs, resolution 2.4&Aring;" />
-'''FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI'''<br />
-==Overview==
+==FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI==
-Folylpolyglutamate 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.
+<StructureSection load='1fgs' size='340' side='right'caption='[[1fgs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fgs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacticaseibacillus_casei Lacticaseibacillus casei]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1FGS FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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=1fgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgs OCA], [https://pdbe.org/1fgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgs RCSB], [https://www.ebi.ac.uk/pdbsum/1fgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgs ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FPGS_LACCA FPGS_LACCA] Involved in the conversion of folates to polyglutamate derivatives, and likely functions in the retention of cellular folate pools. Catalyzes successive MgATP-dependent additions of glutamate to a pteroylmonoglutamate substrate, with a high preference for 5,10-methylenetetrahydrofolate (mTHF). Thus, metabolizes mTHF to the tetraglutamate derivative, but longer glutamate chain length products are not observed. Tetrahydrofolate (H4PteGlu) and 10-formyl-H4PteGlu are poorer folate substrates. In contrast to E.coli FolC, this enzyme does not display dihydrofolate synthase activity.<ref>PMID:18232714</ref> <ref>PMID:6138353</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/1fgs_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fgs ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with MG and POP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGS OCA].
+*[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]]
+== References ==
-==Reference==
+<references/>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9618466 9618466]
+__TOC__
-[[Category: Lactobacillus casei]]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Lacticaseibacillus casei]]
-[[Category: Tetrahydrofolate synthase]]
+[[Category: Large Structures]]
-[[Category: Baker, E.]]
+[[Category: Baker E]]
-[[Category: Bognar, A.]]
+[[Category: Bognar A]]
-[[Category: Smith, C.]]
+[[Category: Smith C]]
-[[Category: Sun, X.]]
+[[Category: Sun X]]
-[[Category: MG]]
-[[Category: POP]]
-[[Category: ligase]]
-[[Category: synthetase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:54:51 2007''