Open AccessX‐ray structure of glutathione S ‐transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate‐binding site
Author(s) -
Rufer Arne Christian,
Thiebach Lars,
Baer Kristin,
Klein Helmut W.,
Hennig Michael
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105004823
Subject(s) - schistosoma japonicum , orthorhombic crystal system , dimer , glutathione s transferase , transferase , chemistry , biology , stereochemistry , crystallography , glutathione , crystal structure , biochemistry , schistosomiasis , enzyme , immunology , helminths , organic chemistry
The crystal structure of the 26 kDa glutathione S ‐transferase from Schistosoma japonicum ( Sj GST) was determined at 3 Å resolution in the new space group P 2 1 2 1 2 1 . The structure of orthorhombic Sj GST reveals unique features of the ligand‐binding site and dimer interface when compared with previously reported structures. Sj GST is recognized as the major detoxification enzyme of S. japonicum , a pathogenic helminth causing schistosomiasis. As resistance against the established inhibitor of Sj GST, praziquantel, has been reported these results might prove to be valuable for the development of novel drugs.