7n79

O2-, PLP-dependent desaturase Plu4 holo-enzyme

spinqualitylabelsall models 7n79, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7n79 is a 2 chain structure with sequence from Pseudoalteromonas luteoviolacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: ACT, BTB, EDO, LLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0C1MLE8_9GAMM Publication Abstract from PubMed The mechanism by which molecular oxygen is activated by the organic cofactor pyridoxal phosphate (PLP) for oxidation reactions remains poorly understood. Recent work has identified arginine oxidases that catalyze desaturation or hydroxylation reactions. Here, we investigate a desaturase from the Pseudoalteromonas luteoviolacea indolmycin pathway. Our work, combining X-ray crystallographic, biochemical, spectroscopic, and computational studies, supports a shared mechanism with arginine hydroxylases, involving two rounds of single-electron transfer to oxygen and superoxide rebound at the 4' carbon of the PLP cofactor. The precise positioning of a water molecule in the active site is proposed to control the final reaction outcome. This proposed mechanism provides a unified framework to understand how oxygen can be activated by PLP-dependent enzymes for oxidation of arginine and elucidates a shared mechanistic pathway and intertwined evolutionary history for arginine desaturases and hydroxylases. A shared mechanistic pathway for pyridoxal phosphate-dependent arginine oxidases.,Hoffarth ER, Caddell Haatveit K, Kuatsjah E, MacNeil GA, Saroya S, Walsby CJ, Eltis LD, Houk KN, Garcia-Borras M, Ryan KS Proc Natl Acad Sci U S A. 2021 Oct 5;118(40). pii: 2012591118. doi:, 10.1073/pnas.2012591118. PMID:34580201 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA