TY - JOUR
T1 - Three-dimensional structure of a Bombyx mori Omega-class glutathione transferase
AU - Yamamoto, Kohji
AU - Suzuki, Mamoru
AU - Higashiura, Akifumi
AU - Nakagawa, Atsushi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan . The work was also supported in part by a Research Grant for Young Investigators of Faculty of Agriculture, Kyushu University . This work was performed under the auspices of the Cooperative Research Program of Institute for Protein Research, Osaka University. The synchrotron radiation experiments were carried out at the BL-5A of Photon Factory (Proposal No. 2012G003) and at the BL44XU of SPring-8 with the approval of JASRI (Proposal Nos. 2012A6756, and 2012B6756).
PY - 2013/9/6
Y1 - 2013/9/6
N2 - Glutathione transferases (GSTs) are major phase II detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here we report the crystal structure of an Omega-class glutathione transferase of Bombyx mori, bmGSTO, to gain insight into its catalytic mechanism. The structure of bmGSTO complexed with glutathione determined at a resolution of 2.5. Å reveals that it exists as a dimer and is structurally similar to Omega-class GSTs with respect to its secondary and tertiary structures. Analysis of a complex between bmGSTO and glutathione showed that bound glutathione was localized to the glutathione-binding site (G-site). Site-directed mutagenesis of bmGSTO mutants indicated that amino acid residues Leu62, Lys65, Lys77, Val78, Glu91 and Ser92 in the G-site contribute to catalytic activity.
AB - Glutathione transferases (GSTs) are major phase II detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here we report the crystal structure of an Omega-class glutathione transferase of Bombyx mori, bmGSTO, to gain insight into its catalytic mechanism. The structure of bmGSTO complexed with glutathione determined at a resolution of 2.5. Å reveals that it exists as a dimer and is structurally similar to Omega-class GSTs with respect to its secondary and tertiary structures. Analysis of a complex between bmGSTO and glutathione showed that bound glutathione was localized to the glutathione-binding site (G-site). Site-directed mutagenesis of bmGSTO mutants indicated that amino acid residues Leu62, Lys65, Lys77, Val78, Glu91 and Ser92 in the G-site contribute to catalytic activity.
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U2 - 10.1016/j.bbrc.2013.08.011
DO - 10.1016/j.bbrc.2013.08.011
M3 - Article
C2 - 23939046
AN - SCOPUS:84883306872
SN - 0006-291X
VL - 438
SP - 588
EP - 593
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -