5zwp

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

spinqualitylabelsall models 5zwp, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zwp is a 2 chain structure with sequence from Musca domestica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: FMT, GSH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSTT1_MUSDO Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Publication Abstract from PubMed 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 1.4A. 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. Crystal structure of the delta-class glutathione transferase in Musca domestica.,Sue M, Yajima S Biochem Biophys Res Commun. 2018 Jul 20;502(3):345-350. doi:, 10.1016/j.bbrc.2018.05.161. Epub 2018 May 30. PMID:29803675 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase 3D structures

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