X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Arne Christian RuferMichael Hennig

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.

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Jan 30, 2003·Acta Crystallographica. Section D, Biological Crystallography·Allan D'ArcyAlexander Haber
Jun 26, 2003·Protein Science : a Publication of the Protein Society·Douglas R SmythBostjan Kobe
May 4, 2004·Trends in Molecular Medicine·Wei HuZe-Guang Han

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Citations

May 24, 2008·The Journal of Biological Chemistry·Elisabetta MantuanoSteven L Gonias
Mar 2, 2013·PloS One·Immacolata LuisiFederico Berti
Mar 30, 2010·Protein Expression and Purification·Young-Hyun HanYong Je Chung
Nov 18, 2008·Protein Expression and Purification·Muluken S BelewSusan M Aitken
Jul 28, 2016·Nature·Marcus D WilsonDaniel Durocher
Jul 22, 2006·The Journal of Biological Chemistry·Thorben Dammeyer, Nicole Frankenberg-Dinkel

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