[1]
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PROTEIN SEQUENCE (ISOZYME 1).
STRAIN=B [RT500];
PubMed=320005 [NCBI, ExPASy, EBI, Israel, Japan]
Stone D.,
Phillips A.W.,
Burchall J.J.;
"The amino-acid sequence of the dihydrofolate reductase of a trimethoprim-resistant strain of Escherichia coli.";
Eur. J. Biochem. 72:613-624(1977).
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[2]
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PROTEIN SEQUENCE.
STRAIN=B [MB1428];
DOI=10.1021/bi00600a030; PubMed=350268 [NCBI, ExPASy, EBI, Israel, Japan]
Bennett C.D.,
Rodkey J.A.,
Sondey J.M.,
Hirschmann R.;
"Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.";
Biochemistry 17:1328-1337(1978).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/8.10.2255; PubMed=6159575 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.R.,
Calvo J.M.;
"Nucleotide sequence of the E coli gene coding for dihydrofolate reductase.";
Nucleic Acids Res. 8:2255-2274(1980).
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[4]
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PROTEIN SEQUENCE (ISOZYME 2).
STRAIN=B [RT500];
PubMed=7007370 [NCBI, ExPASy, EBI, Israel, Japan]
Baccanari D.P.,
Stone D.,
Kuyper L.;
"Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.";
J. Biol. Chem. 256:1738-1747(1981).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1810;
PubMed=3549289 [NCBI, ExPASy, EBI, Israel, Japan]
Flensburg J.,
Skoeld O.;
"Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim.";
Eur. J. Biochem. 162:473-476(1987).
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[6]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T.,
Mori H.,
Nagai H.,
Nagata T.,
Ishihama A.,
Fujita N.,
Isono K.,
Mizobuchi K.,
Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
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[7]
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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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[8]
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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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[9]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=6815179 [NCBI, ExPASy, EBI, Israel, Japan]
Filman D.J.,
Bolin J.T.,
Matthews D.A.,
Kraut J.;
"Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7-A resolution. II. Environment of bound NADPH and implications for catalysis.";
J. Biol. Chem. 257:13663-13672(1982).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi00465a018; PubMed=2185835 [NCBI, ExPASy, EBI, Israel, Japan]
Bystroff C.,
Oatley S.J.,
Kraut J.;
"Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state.";
Biochemistry 29:3263-3277(1990).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1021/bi00222a028; PubMed=1998681 [NCBI, ExPASy, EBI, Israel, Japan]
Bystroff C.,
Kraut J.;
"Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding.";
Biochemistry 30:2227-2239(1991).
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