1fgs: Difference between revisions

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-[[Image:1fgs.gif|left|200px]]
-<!--
+==FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI==
-The line below this paragraph, containing "STRUCTURE_1fgs", creates the "Structure Box" on the page.
+<StructureSection load='1fgs' size='340' side='right'caption='[[1fgs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1fgs|  PDB=1fgs  |  SCENE=  }}
+<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>
-'''FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI'''
+==See Also==
+*[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Lacticaseibacillus casei]]
-FGS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGS OCA].
+[[Category: Large Structures]]
+[[Category: Baker E]]
-==Reference==
+[[Category: Bognar A]]
-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://www.ncbi.nlm.nih.gov/pubmed/9618466 9618466]
+[[Category: Smith C]]
-[[Category: Lactobacillus casei]]
+[[Category: Sun X]]
-[[Category: Single protein]]
-[[Category: Tetrahydrofolate synthase]]
-[[Category: Baker, E.]]
-[[Category: Bognar, A.]]
-[[Category: Smith, C.]]
-[[Category: Sun, X.]]
-[[Category: Ligase]]
-[[Category: Synthetase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:18:31 2008''