X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site.
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.
Rufer
Arne Christian
AC
F. Hoffmann-La Roche AG, Pharma Research Discovery Chemistry, 4070 Basel, Switzerland. arne.rufer@roche.com
Thiebach
Lars
L
Baer
Kristin
K
Klein
Helmut W
HW
Hennig
Michael
M
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
D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase