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[[Image:1fgs.gif|left|200px]]


{{Structure
==FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI==
|PDB= 1fgs |SIZE=350|CAPTION= <scene name='initialview01'>1fgs</scene>, resolution 2.4&Aring;
<StructureSection load='1fgs' size='340' side='right'caption='[[1fgs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
<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>
|ACTIVITY= [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]  
</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>
|GENE=  
<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>


'''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]]
1FGS 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: MG]]
[[Category: POP]]
[[Category: ligase]]
[[Category: synthetase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:53 2008''

Latest revision as of 10:14, 7 February 2024

FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEIFOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI

Structural highlights

1fgs is a 1 chain structure with sequence from Lacticaseibacillus casei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Sheng Y, Khanam N, Tsaksis Y, Shi XM, Lu QS, Bognar AL. Mutagenesis of folylpolyglutamate synthetase indicates that dihydropteroate and tetrahydrofolate bind to the same site. Biochemistry. 2008 Feb 26;47(8):2388-96. PMID:18232714 doi:10.1021/bi701670y
  2. ↑ Bognar AL, Shane B. Purification and properties of Lactobacillus casei folylpoly-gamma-glutamate synthetase. J Biol Chem. 1983 Oct 25;258(20):12574-81 PMID:6138353

1fgs, resolution 2.40Å

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