TY - JOUR
T1 - New insights into the catalytic mechanism of Bombyx mori prostaglandin e synthase gained from structure-function analysis
AU - Yamamoto, Kohji
AU - Suzuki, Mamoru
AU - Higashiura, Akifumi
AU - Aritake, Kosuke
AU - Urade, Yoshihiro
AU - Uodome, Nobuko
AU - Hossain, Tofazzal
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 . 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. 2012G001 and 2012G003) and at the BL44XU of SPring-8 with the approval of JASRI (Proposal No. 2012A6756, and 2012B6756).
PY - 2013/11/1
Y1 - 2013/11/1
N2 - Prostaglandin E synthase (PGES) catalyzes the isomerization of PGH 2 to PGE2. We previously reported the identification and structural characterization of Bombyx mori PGES (bmPGES), which belongs to Sigma-class glutathione transferase. Here, we extend these studies by determining the structure of bmPGES in complex with glutathione sulfonic acid (GTS) at a resolution of 1.37 Å using X-ray crystallography. GTS localized to the glutathione-binding site. We found that electron-sharing network of bmPGES includes Asn95, Asp96, and Arg98. Site-directed mutagenesis of these residues to create mutant forms of bmPGES mutants indicate that they contribute to catalytic activity. These results are, to our knowledge, the first to reveal the presence of an electron-sharing network in bmPGES.
AB - Prostaglandin E synthase (PGES) catalyzes the isomerization of PGH 2 to PGE2. We previously reported the identification and structural characterization of Bombyx mori PGES (bmPGES), which belongs to Sigma-class glutathione transferase. Here, we extend these studies by determining the structure of bmPGES in complex with glutathione sulfonic acid (GTS) at a resolution of 1.37 Å using X-ray crystallography. GTS localized to the glutathione-binding site. We found that electron-sharing network of bmPGES includes Asn95, Asp96, and Arg98. Site-directed mutagenesis of these residues to create mutant forms of bmPGES mutants indicate that they contribute to catalytic activity. These results are, to our knowledge, the first to reveal the presence of an electron-sharing network in bmPGES.
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U2 - 10.1016/j.bbrc.2013.10.001
DO - 10.1016/j.bbrc.2013.10.001
M3 - Article
C2 - 24120949
AN - SCOPUS:84887064343
SN - 0006-291X
VL - 440
SP - 762
EP - 767
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -