7BIB

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

Summary for 7BIB

• Entry DOI: 10.2210/pdb7bib/pdb
• Descriptor: Glutathione S-transferase A1, (2~{R})-2-azanyl-5-[[(2~{R})-3-(hexylcarbamothioylsulfanyl)-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid (3 entities in total)
• Functional Keywords: glutathione transferase, ligandin, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 52241.39

Authors

Schwartz, M.,Neiers, F. (deposition date: 2021-01-12, release date: 2022-03-02, Last modification date: 2024-01-31)

Primary citation

Schwartz, M.,Brignot, H.,Feron, G.,Hummel, T.,Zhu, Y.,von Koskull, D.,Heydel, J.M.,Lirussi, F.,Canon, F.,Neiers, F.
Role of human salivary enzymes in bitter taste perception.
Food Chem, 386:132798-132798, 2022

PubMed Abstract: The molecules that elicit taste sensation are perceived by interacting with the taste receptors located in the taste buds. Enzymes involved in the detoxification processes are found in saliva as well as in type II cells, where taste receptors, including bitter taste receptors, are located. These enzymes are known to interact with a large panel of molecules. To explore a possible link between these enzymes and bitter taste perception, we demonstrate that salivary glutathione transferases (GSTA1 and GSTP1) can metabolize bitter molecules. To support these abilities, we solve three X-ray structures of these enzymes in complexes with isothiocyanates. Salivary GSTA1 and GSTP1 are expressed in a large panel of subjects. Additionally, GSTA1 levels in the saliva of people suffering from taste disorders are significantly lower than those in the saliva of the control group.

PubMed: 35344726
DOI: 10.1016/j.foodchem.2022.132798

Experimental method

X-RAY DIFFRACTION (2.03 Å)