1fgs | pdb_00001fgs

FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI

spinqualitylabelsall models 1fgs, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fgs is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, POP Activity: Tetrahydrofolate synthase, with EC number 6.3.2.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Folypolyglutamate synthase

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