3wqg

D-threo-3-hydroxyaspartate dehydratase C353A mutant in the metal-free form

spinqualitylabelsall models 3wqg, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wqg is a 2 chain structure with sequence from Delftia sp. HT23. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: GOL, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DTHAD_DELSH Publication Abstract from PubMed D-threo-3-Hydroxyaspartate dehydratase (D-THA DH) is a fold-type III pyridoxal 5'-phosphate-dependent enzyme, isolated from a soil bacterium of Delftia sp. HT23. It catalyzes the dehydration of D-threo-3-hydroxyaspartate (D-THA) and L-erythro-3-hydroxyaspartate (L-EHA). To elucidate the mechanism of substrate stereospecificity, crystal structures of D-THA DH were determined in complex with various ligands, such as an inhibitor (D-erythro-3-hydroxyaspartate (D-EHA)), a substrate (L-EHA), and the reaction intermediate (2-amino maleic acid). The C beta -OH of L-EHA occupied a position close to the active-site Mg2+, clearly indicating a possibility of metal-assisted C beta -OH elimination from the substrate. In contrast, the C beta -OH of an inhibitor was bound far from the active-site Mg2+. This suggests that the substrate specificity of D-THA DH is determined by the orientation of the C beta -OH at the active site, whose spatial arrangement is compatible with the 3R configuration of 3-hydroxyaspartate. We also report an optically pure synthesis of L-threo-3-hydroxyaspartate (L-THA) and D-EHA, promising intermediates for the synthesis of beta-benzyloxyaspartate, by using a purified D-THA DH as a biocatalyst for the resolution of racemic DL-threo-3-hydroxyaspartate (DL-THA) and DL-erythro-3-hydroxyaspartate (DL-EHA). Considering 50 % of the theoretical maximum, efficient yields of L-THA (38.9 %) and D-EHA (48.9 %) as isolated crystals were achieved with >99 % enantiomeric excess (e.e.). The results of nuclear magnetic resonance signals verified the chemical purity of the products. We were directly able to isolate analytically pure compounds by the recrystallization of acidified reaction mixtures (pH 2.0) and thus avoiding the use of environmentally harmful organic solvents for the chromatographic purification. Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate.,Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M Appl Microbiol Biotechnol. 2015 Feb 26. PMID:25715785 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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