[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B;
DOI=10.1093/nar/12.24.9299; PubMed=6393055 [NCBI, ExPASy, EBI, Israel, Japan]
Gushima H.,
Yasuda S.,
Soeda E.,
Yokota M.,
Kondo M.,
Kimura A.;
"Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II.";
Nucleic Acids Res. 12:9299-9307(1984).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
STRAIN=B;
DOI=10.1006/jmbi.1993.1106; PubMed=8445637 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi H.,
Kato H.,
Hata Y.,
Nishioka T.,
Kimura A.,
Oda J.,
Katsube Y.;
"Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0-A resolution.";
J. Mol. Biol. 229:1083-1100(1993).
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[5]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
STRAIN=B;
DOI=10.1093/protein/9.12.1083; PubMed=9010922 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuda K.,
Mizuguchi K.,
Nishioka T.,
Kato H.,
Go N.,
Oda J.;
"Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.";
Protein Eng. 9:1083-1092(1996).
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[6]
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MUTAGENESIS OF PRO-227 AND GLY-240.
DOI=10.1021/bi00097a018; PubMed=8241129 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T.,
Yamaguchi H.,
Kato H.,
Nishioka T.,
Katsube Y.,
Oda J.;
"Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase.";
Biochemistry 32:12398-12404(1993).
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[7]
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PROTEIN SEQUENCE OF 234-242, AND MUTAGENESIS OF ARG-233 AND ARG-241.
STRAIN=B;
DOI=10.1021/bi00123a007; PubMed=1540581 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T.,
Kato H.,
Nishioka T.,
Oda J.;
"Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction.";
Biochemistry 31:2259-2265(1992).
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[8]
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MUTAGENESIS OF CYSTEINE RESIDUES.
STRAIN=B;
PubMed=3042775 [NCBI, ExPASy, EBI, Israel, Japan]
Kato H.,
Tanaka T.,
Nishioka T.,
Kimura A.,
Oda J.;
"Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis.";
J. Biol. Chem. 263:11646-11651(1988).
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