title: X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site.
abstract: The crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum (SjGST) was determined at 3 A resolution in the new space group P2(1)2(1)2(1). The structure of orthorhombic SjGST reveals unique features of the ligand-binding site and dimer interface when compared with previously reported structures. SjGST is recognized as the major detoxification enzyme of S. japonicum, a pathogenic helminth causing schistosomiasis. As resistance against the established inhibitor of SjGST, praziquantel, has been reported these results might prove to be valuable for the development of novel drugs.
authors.affiliation: F. Hoffmann-La Roche AG, Pharma Research Discovery Chemistry, 4070 Basel, Switzerland. arne.rufer@roche.com
authors.forename: Arne Christian
authors.initials: AC
authors.lastname: Rufer
authors.forename: Lars
authors.initials: L
authors.lastname: Thiebach
authors.forename: Kristin
authors.initials: K
authors.lastname: Baer
authors.forename: Helmut W
authors.initials: HW
authors.lastname: Klein
authors.forename: Michael
authors.initials: M
authors.lastname: Hennig
mesh_terms: D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D019281:Dimerization; D005982:Glutathione Transferase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008958:Models, Molecular; D008970:Molecular Weight; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012549:Schistosoma japonicum / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase