6yaw

Crystal structure of human GSTA1-1 bound to the glutathione adduct of cinnamaldehyde

spinqualitylabelsall models 6yaw, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yaw is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.19Å Ligands: GOL, P9H Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSTA1_HUMAN Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Publication Abstract from PubMed Xenobiotic metabolizing enzymes and other proteins, including odorant-binding proteins located in the nasal epithelium and mucus, participate in a series of processes modulating the concentration of odorants in the environment of olfactory receptors and finely impact odor perception. These enzymes and transporters are thought to participate in odorant degradation or transport. Odorant biotransformation results in (i) changes in the odorant quantity up to their clearance and the termination of signalling and (ii) the formation of new odorant stimuli (metabolites). Enzymes, such as cytochrome P450 and glutathione transferases (GSTs), have been proposed to participate in odorant clearance in insects and mammals as odorant metabolizing enzymes. This study aims to explore the function of GSTs in human olfaction. Using immunohistochemical methods, GSTs were found to be localized in human tissues surrounding the olfactory epithelium. Then, the activity of two members of the GST family towards odorants was measured using heterologously expressed enzymes. The interactions/reactions with odorants were further characterized using a combination of enzymatic techniques. Furthermore, the structure of the complex between human GSTA1 and the glutathione conjugate of an odorant was determined by X-ray crystallography. Our results strongly suggest the role of human GSTs in the modulation of odorant availability to olfactory receptors in the peripheral olfactory process. Interactions between Odorants and Glutathione Transferases in the Human Olfactory Cleft.,Schwartz M, Menetrier F, Heydel JM, Chavanne E, Faure P, Labrousse M, Lirussi F, Canon F, Mannervik B, Briand L, Neiers F Chem Senses. 2020 Aug 21. pii: 5895478. doi: 10.1093/chemse/bjaa055. PMID:32822468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase 3D structures

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