RRC ID |
30570
|
著者 |
Yamamoto K, Suzuki M, Higashiura A, Nakagawa A.
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タイトル |
Three-dimensional structure of a Bombyx mori Omega-class glutathione transferase.
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ジャーナル |
Biochem Biophys Res Commun
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Abstract |
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 2.5Å 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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巻・号 |
438(4)
|
ページ |
588-93
|
公開日 |
2013-9-6
|
DOI |
10.1016/j.bbrc.2013.08.011
|
PII |
S0006-291X(13)01327-2
|
PMID |
23939046
|
MeSH |
Animals
Binding Sites
Bombyx / chemistry
Bombyx / enzymology*
Bombyx / genetics
Bombyx / metabolism
Catalytic Domain
Crystallography, X-Ray
Glutathione / metabolism
Glutathione Transferase / chemistry*
Glutathione Transferase / genetics
Glutathione Transferase / metabolism*
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation
Protein Multimerization
|
IF |
2.985
|
引用数 |
13
|
WOS 分野
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
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リソース情報 |
カイコ |
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