5a4d

Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP

spinqualitylabelsall models 5a4d, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a4d is a 8 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: KZH, NAP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function QORH_ARATH Publication Abstract from PubMed Enzymatic and non-enzymatic peroxidation of polyunsaturated fatty acids give rise to accumulation of aldehydes, ketones, and alpha,beta-unsaturated carbonyls of various lengths, known as oxylipins. Oxylipins with alpha,beta-unsaturated carbonyls are reactive electrophile species and are toxic. Cells have evolved several mechanisms to scavenge reactive electrophile oxylipins and decrease their reactivity such as by coupling with glutathione, or by reduction using NAD(P)H-dependent reductases and dehydrogenases of various substrate specificities. Plant cell chloroplasts produce reactive electrophile oxylipins named gamma-ketols downstream of enzymatic lipid peroxidation. The chloroplast envelope quinone oxidoreductase homolog (ceQORH) from Arabidopsis thaliana was previously shown to reduce the reactive double bond of gamma-ketols. In marked difference with its cytosolic homolog alkenal reductase (AtAER) that displays a high activity toward the ketodiene 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE) and the ketotriene 13-oxo-9(Z), 11(E), 15(Z)-octadecatrienoic acid (13-KOTE), ceQORH binds, but does not reduce, 13-KODE and 13-KOTE. Crystal structures of apo-ceQORH and ceQORH bound to 13-KOTE or to NADP+ and 13-KOTE have been solved showing a large ligand binding site, also observed in the structure of the cytosolic alkenal/one reductase. Positioning of the alpha,beta-unsaturated carbonyl of 13-KOTE in ceQORH-NADP+-13-KOTE, far away from the NADP+ nicotinamide ring, provides a rational for the absence of activity with the ketodienes and ketotrienes. ceQORH is a monomeric enzyme in solution whereas other enzymes from the quinone oxidoreductase family are stable dimers and a structural explanation of this difference is proposed. A possible in vivo role of ketodienes and ketotrienes binding to ceQORH is also discussed. Crystal Structure of the Chloroplastic Oxoene Reductase ceQORH from Arabidopsis thaliana.,Mas Y Mas S, Curien G, Giustini C, Rolland N, Ferrer JL, Cobessi D Front Plant Sci. 2017 Mar 9;8:329. doi: 10.3389/fpls.2017.00329. eCollection, 2017. PMID:28337214 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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