2xua

Crystal structure of the enol-lactonase from Burkholderia xenovorans LB400

spinqualitylabelsall models 2xua, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xua is a 2 chain structure with sequence from Paraburkholderia xenovorans LB400. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: MSE, SHF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q13KT2_PARXL Publication Abstract from PubMed Lactones are a class of structurally diverse molecules that serve essential roles in biological processes ranging from quorum sensing to the aerobic catabolism of aromatic compounds. Not surprisingly, enzymes involved in the bioprocessing of lactones are often targeted for protein engineering studies with the potential, for example, of optimized bioremediation of aromatic pollutants. The enol-lactone hydrolase (ELH) represents one such class of targeted enzymes and catalyzes the conversion of 3-oxoadipate-enol-lactone into the linear beta-ketoadipate. To define the structural details that govern ELH catalysis and assess the impact of divergent features predicted by sequence analysis, we report the first structural characterization of an ELH (PcaD) from Burkholderia xenovorans LB400 in complex with the product analog levulinic acid. The overall dimeric structure of PcaD reveals an alpha-helical cap domain positioned atop a core alpha/beta-hydrolase domain. Despite the localization of the conserved catalytic triad to the core domain, levulinic acid is bound largely within the region of the active site defined by the cap domain, suggesting a key role for this divergent substructure in mediating product release. Furthermore, the architecture of the cap domain results in an unusually deep active-site pocket with topological features to restrict binding to small or kinked substrates. The evolutionary basis for this substrate selectivity is discussed with respect to the homologous dienelactone hydrolase. Overall, the PcaD costructure provides a detailed insight into the intimate role of the cap domain in influencing all aspects of substrate binding, turnover, and product release. A Product Analog Bound Form of 3-Oxoadipate-enol-Lactonase (PcaD) Reveals a Multifunctional Role for the Divergent Cap Domain.,Bains J, Kaufman L, Farnell B, Boulanger MJ J Mol Biol. 2011 Jan 13. PMID:21237173 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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