5v2d

Crystal structure of Pseudomonas brassicacearum lignostilbene dioxygenaseCrystal structure of Pseudomonas brassicacearum lignostilbene dioxygenase

Structural highlights 5v2d is a 4 chain structure with sequence from Pseudomonas brassicacearum. 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: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8QAY8_9PSED Publication Abstract from PubMed BACKGROUND: Stilbene cleaving oxygenases (SCOs), also known as lignostilbene-alpha,beta-dioxygenases (LSDs) mediate the oxidative cleavage of the olefinic double bonds of lignin-derived intermediate phenolic stilbenes, yielding small modified benzaldehyde compounds. SCOs represent one branch of the larger carotenoid cleavage oxygenases family. Here, we describe the structural and functional characterization of an SCO-like enzyme from the soil-born, bio-control agent Pseudomonas brassicacearum. METHODS: In vitro and in vivo assays relying on visual inspection, spectrophotometric quantification, as well as liquid-chormatographic and mass spectrometric characterization were applied for functional evaluation of the enzyme. X-ray crystallographic analyses and in silico modeling were applied for structural investigations. RESULTS: In vitro assays demonstrated preferential cleavage of resveratrol, while in vivo analyses detected putative cleavage of the straight chain carotenoid, lycopene. A high-resolution structure containing the seven-bladed beta-propeller fold and conserved 4-His-Fe unit at the catalytic site, was obtained. Comparative structural alignments, as well as in silico modelling and docking, highlight potential molecular factors contributing to both the primary in vitro activity against resveratrol, as well as the putative subsidiary activities against carotenoids in vivo, for future validation. CONCLUSIONS: The findings reported here provide validation of the SCO structure, and highlight enigmatic points with respect to the potential effect of the enzyme's molecular environment on substrate specificities for future investigation. Structure and function of a lignostilbene-alpha,beta-dioxygenase orthologue from Pseudomonas brassicacearum.,Loewen PC, Switala J, Wells JP, Huang F, Zara AT, Allingham JS, Loewen MC BMC Biochem. 2018 Aug 16;19(1):8. doi: 10.1186/s12858-018-0098-4. PMID:30115012 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5v2d, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image