5ZWP

Crystal structure of the delta-class glutathione transferase from Musca domestica

Summary for 5ZWP

• Entry DOI: 10.2210/pdb5zwp/pdb
• Descriptor: Glutathione S-transferase 1, GLUTATHIONE, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: isozyme, detoxification, housefly, gst, transferase
• Biological source: Musca domestica (House fly)
• Total number of polymer chains: 2
• Total formula weight: 48409.47

Authors

Sue, M.,Yajima, S. (deposition date: 2018-05-16, release date: 2018-06-13, Last modification date: 2023-11-22)

Primary citation

Sue, M.,Yajima, S.
Crystal structure of the delta-class glutathione transferase in Musca domestica
Biochem. Biophys. Res. Commun., 502:345-350, 2018

PubMed Abstract: Among the various glutathione transferase (GST) isozymes in insects, the delta- and epsilon-class GSTs fulfill critical functions during the detoxification of insecticides. We crystalized MdGSTD1, the major delta-class GST isozyme in the housefly (Musca domestica), in complex with glutathione (GSH) and solved its structure at a resolution of 1.4 Å. The overall folding of MdGSTD1 resembled other known delta-class GSTs. Its substrate binding pocket was exposed to solvent and considerably more open than in the epsilon-class GST from M. domestica (MdGSTE2). However, their C-terminal structures differed the most because of the different lengths of the C-terminal regions. Although this region does not seem to directly interact with substrates, its deletion reduced the enzymatic activity by more than 70%, indicating a function in maintaining the proper conformation of the binding pocket. Binding of GSH to the GSH-binding region of MdGSTD1 results in a rigid conformation of this region. Although MdGSTD1 has a higher affinity for GSH than the epsilon class enzymes, the thiol group of the GSH molecule was not close enough to serine residue 9 to form a hydrogen-bond with this residue, which is predicted to act as the catalytic center for thiol group deprotonation in GSH.

PubMed: 29803675
DOI: 10.1016/j.bbrc.2018.05.161

Experimental method

X-RAY DIFFRACTION (1.4 Å)