3cwn | pdb_00003cwn

Escherichia coli transaldolase b mutant f178y

spinqualitylabelsall models 3cwn, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cwn is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 1onr Gene: talB, yaaK ("Bacillus coli" Migula 1895) Activity: Transaldolase, with EC number 2.2.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TALB_ECOLI] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.[HAMAP-Rule:MF_00492] 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 Based on a structure-assisted sequence alignment we designed 11 focused libraries at residues in the active site of transaldolase B from Escherichia coli and screened them for their ability to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate using a newly developed color assay. We found one positive variant exhibiting a replacement of Phe(178) to Tyr. This mutant variant is able not only to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate (14 units/mg), but to use it as a substrate directly in an aldolase reaction (7 units/mg). With a single amino acid replacement the fructose-6-phosphate aldolase activity was increased considerably (>70-fold compared with wild-type). Structural studies of the wild-type and mutant protein suggest that this is due to a different H-bond pattern in the active site leading to a destabilization of the Schiff base intermediate. Furthermore, we show that a homologous replacement has a similar effect in the human transaldolase Taldo1 (aldolase activity, 14 units/mg). We also demonstrate that both enzymes TalB and Taldo1 are recognized by the same polyclonal antibody. Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin.,Schneider S, Sandalova T, Schneider G, Sprenger GA, Samland AK J Biol Chem. 2008 Oct 31;283(44):30064-72. Epub 2008 Aug 7. PMID:18687684 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transaldolase

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