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P0ABQ4

- DYR_ECOLI

UniProt

P0ABQ4 - DYR_ECOLI

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Protein

Dihydrofolate reductase

Gene

folA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.1 PublicationPROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51Substrate; via carbonyl oxygen
Binding sitei7 – 71NADP; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei27 – 271Substrate
Binding sitei52 – 521Substrate
Binding sitei57 – 571Substrate
Binding sitei76 – 761NADP; via carbonyl oxygen1 Publication
Binding sitei113 – 1131Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 197NADP1 Publication
Nucleotide bindingi45 – 462NADP1 Publication
Nucleotide bindingi63 – 642NADP1 Publication
Nucleotide bindingi95 – 1028NADP1 Publication

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: EcoCyc
  2. NADP binding Source: InterPro

GO - Biological processi

  1. 10-formyltetrahydrofolate biosynthetic process Source: EcoCyc
  2. folic acid biosynthetic process Source: EcoCyc
  3. glycine biosynthetic process Source: InterPro
  4. nucleotide biosynthetic process Source: InterPro
  5. one-carbon metabolic process Source: UniProtKB-KW
  6. response to antibiotic Source: UniProtKB-KW
  7. response to drug Source: EcoliWiki
  8. response to methotrexate Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:DIHYDROFOLATEREDUCT-MONOMER.
ECOL316407:JW0047-MONOMER.
MetaCyc:DIHYDROFOLATEREDUCT-MONOMER.
SABIO-RKP0ABQ4.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:folA
Synonyms:tmrA
Ordered Locus Names:b0048, JW0047
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10326. folA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161M → F or S: Increases catalytic rate about 2-fold. 1 Publication
Mutagenesisi16 – 161M → N: Increases catalytic rate about 2-fold. Increases catalytic rate about 7-fold; when associated with L-20; Y-42; F-92; A-85 and S-152. 1 Publication
Mutagenesisi20 – 201M → I or V: Increases catalytic rate 2-fold. 1 Publication
Mutagenesisi20 – 201M → L: Increases catalytic rate 2.5-fold. Increases catalytic rate about 7-fold; when associated with N-16; Y-42; F-92; A-85 and S-152. 1 Publication
Mutagenesisi42 – 421M → V: Increases catalytic rate almost 2-fold. 1 Publication
Mutagenesisi42 – 421M → Y: Increases catalytic rate almost 2-fold. Increases catalytic rate about 7-fold; when associated with N-16; L-20; A-85; F-92 and S-152. 1 Publication
Mutagenesisi85 – 851C → A: Decreases catalytic rate by one third. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; F-92 and S-152. 1 Publication
Mutagenesisi92 – 921M → F: No effect. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; A-85 and S-152. 1 Publication
Mutagenesisi92 – 921M → L: No effect. 1 Publication
Mutagenesisi152 – 1521C → S: Increases catalytic rate 1.5-fold. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; A-85 and F-92. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 159159Dihydrofolate reductasePRO_0000186387Add
BLAST

Proteomic databases

PaxDbiP0ABQ4.
PRIDEiP0ABQ4.

2D gel databases

SWISS-2DPAGEP0ABQ4.

Expressioni

Gene expression databases

GenevestigatoriP0ABQ4.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
flxAP776094EBI-550404,EBI-553024

Protein-protein interaction databases

DIPiDIP-35824N.
IntActiP0ABQ4. 16 interactions.
MINTiMINT-1239602.
STRINGi511145.b0048.

Structurei

Secondary structure

1
159
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98
Helixi10 – 123
Beta strandi13 – 164
Turni17 – 193
Helixi25 – 3511
Beta strandi40 – 434
Helixi44 – 507
Beta strandi55 – 573
Beta strandi59 – 624
Beta strandi72 – 776
Helixi78 – 858
Beta strandi91 – 933
Helixi97 – 1037
Helixi104 – 1063
Beta strandi108 – 1158
Beta strandi122 – 1243
Helixi130 – 1323
Beta strandi133 – 1419
Beta strandi147 – 1493
Beta strandi151 – 1588

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DDRX-ray2.45A/B1-159[»]
1DDSX-ray2.20A/B1-159[»]
1DHIX-ray1.90A/B1-159[»]
1DHJX-ray1.80A/B1-159[»]
1DRAX-ray1.90A/B1-159[»]
1DRBX-ray1.96A/B1-159[»]
1DREX-ray2.60A1-159[»]
1DRHX-ray2.30A1-159[»]
1DYHX-ray1.90A/B1-159[»]
1DYIX-ray1.90A/B1-159[»]
1DYJX-ray1.85A/B1-159[»]
1JOLX-ray1.96A/B1-159[»]
1JOMX-ray1.90A1-159[»]
1RA1X-ray1.90A1-159[»]
1RA2X-ray1.60A1-159[»]
1RA3X-ray1.80A1-159[»]
1RA8X-ray1.80A1-159[»]
1RA9X-ray1.55A1-159[»]
1RB2X-ray2.10A/B1-159[»]
1RB3X-ray2.30A/B1-159[»]
1RC4X-ray1.90A1-159[»]
1RD7X-ray2.60A/B1-159[»]
1RE7X-ray2.60A/B1-159[»]
1RF7X-ray1.80A1-159[»]
1RG7X-ray2.00A1-159[»]
1RH3X-ray2.40A1-159[»]
1RX1X-ray2.00A1-159[»]
1RX2X-ray1.80A1-159[»]
1RX3X-ray2.20A1-159[»]
1RX4X-ray2.20A1-159[»]
1RX5X-ray2.30A1-159[»]
1RX6X-ray2.00A1-159[»]
1RX7X-ray2.30A1-159[»]
1RX8X-ray2.80A1-159[»]
1RX9X-ray1.90A1-159[»]
1TDRX-ray2.50A/B1-159[»]
2ANOX-ray2.68A1-159[»]
2ANQX-ray2.13A1-159[»]
2D0KX-ray1.90A/B2-159[»]
2DRCX-ray1.90A/B1-159[»]
2INQneutron diffraction2.20A/B1-159[»]
3DAUX-ray1.50A1-159[»]
3DRCX-ray1.90A/B1-159[»]
3K74X-ray1.95A1-159[»]
3KFYX-ray2.08A1-159[»]
3OCHX-ray1.79A/B1-159[»]
3QL3X-ray1.80A1-159[»]
3QYLX-ray1.79A1-159[»]
3QYOX-ray2.09A1-159[»]
3R33X-ray2.09A1-159[»]
4DFRX-ray1.70A/B1-159[»]
4EIGX-ray2.50A1-159[»]
4EIZX-ray2.20A/B1-159[»]
4EJ1X-ray1.75A/B1-159[»]
4FHBX-ray2.80A1-159[»]
4GH8X-ray1.85A/B1-158[»]
4I13X-ray1.60A1-159[»]
4I1NX-ray1.89A1-159[»]
4KJJX-ray1.15A1-159[»]
4KJKX-ray1.35A1-159[»]
4KJLX-ray1.38A1-159[»]
4NX6X-ray1.35A1-159[»]
4NX7X-ray1.15A1-159[»]
5DFRX-ray2.30A1-159[»]
6DFRX-ray2.40A1-159[»]
7DFRX-ray2.50A1-159[»]
DisProtiDP00301.
ProteinModelPortaliP0ABQ4.
SMRiP0ABQ4. Positions 1-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABQ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 158158DHFRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0262.
HOGENOMiHOG000040233.
InParanoidiP0ABQ4.
KOiK00287.
OMAiCITHVEA.
OrthoDBiEOG6KT2V2.
PhylomeDBiP0ABQ4.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABQ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI
60 70 80 90 100
GRPLPGRKNI ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY
110 120 130 140 150
EQFLPKAQKL YLTHIDAEVE GDTHFPDYEP DDWESVFSEF HDADAQNSHS

YCFEILERR
Length:159
Mass (Da):17,999
Last modified:July 21, 1986 - v1
Checksum:i6A03CDCD7F5F8562
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281L → R in strain: B[RT500] isozyme 2.
Natural varianti30 – 301W → G in strain: 1810.
Natural varianti154 – 1541E → K in strain: B[MB1428].
Natural varianti154 – 1541E → Q in strain: 1810.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01609 Genomic DNA. Translation: AAA87976.1.
X05108 Genomic DNA. Translation: CAA28755.1.
U00096 Genomic DNA. Translation: AAC73159.1.
AP009048 Genomic DNA. Translation: BAB96616.1.
PIRiA93704. RDECD.
RefSeqiNP_414590.1. NC_000913.3.
YP_488354.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73159; AAC73159; b0048.
BAB96616; BAB96616; BAB96616.
GeneIDi12933205.
944790.
KEGGiecj:Y75_p0048.
eco:b0048.
PATRICi32115195. VBIEscCol129921_0049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01609 Genomic DNA. Translation: AAA87976.1 .
X05108 Genomic DNA. Translation: CAA28755.1 .
U00096 Genomic DNA. Translation: AAC73159.1 .
AP009048 Genomic DNA. Translation: BAB96616.1 .
PIRi A93704. RDECD.
RefSeqi NP_414590.1. NC_000913.3.
YP_488354.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DDR X-ray 2.45 A/B 1-159 [» ]
1DDS X-ray 2.20 A/B 1-159 [» ]
1DHI X-ray 1.90 A/B 1-159 [» ]
1DHJ X-ray 1.80 A/B 1-159 [» ]
1DRA X-ray 1.90 A/B 1-159 [» ]
1DRB X-ray 1.96 A/B 1-159 [» ]
1DRE X-ray 2.60 A 1-159 [» ]
1DRH X-ray 2.30 A 1-159 [» ]
1DYH X-ray 1.90 A/B 1-159 [» ]
1DYI X-ray 1.90 A/B 1-159 [» ]
1DYJ X-ray 1.85 A/B 1-159 [» ]
1JOL X-ray 1.96 A/B 1-159 [» ]
1JOM X-ray 1.90 A 1-159 [» ]
1RA1 X-ray 1.90 A 1-159 [» ]
1RA2 X-ray 1.60 A 1-159 [» ]
1RA3 X-ray 1.80 A 1-159 [» ]
1RA8 X-ray 1.80 A 1-159 [» ]
1RA9 X-ray 1.55 A 1-159 [» ]
1RB2 X-ray 2.10 A/B 1-159 [» ]
1RB3 X-ray 2.30 A/B 1-159 [» ]
1RC4 X-ray 1.90 A 1-159 [» ]
1RD7 X-ray 2.60 A/B 1-159 [» ]
1RE7 X-ray 2.60 A/B 1-159 [» ]
1RF7 X-ray 1.80 A 1-159 [» ]
1RG7 X-ray 2.00 A 1-159 [» ]
1RH3 X-ray 2.40 A 1-159 [» ]
1RX1 X-ray 2.00 A 1-159 [» ]
1RX2 X-ray 1.80 A 1-159 [» ]
1RX3 X-ray 2.20 A 1-159 [» ]
1RX4 X-ray 2.20 A 1-159 [» ]
1RX5 X-ray 2.30 A 1-159 [» ]
1RX6 X-ray 2.00 A 1-159 [» ]
1RX7 X-ray 2.30 A 1-159 [» ]
1RX8 X-ray 2.80 A 1-159 [» ]
1RX9 X-ray 1.90 A 1-159 [» ]
1TDR X-ray 2.50 A/B 1-159 [» ]
2ANO X-ray 2.68 A 1-159 [» ]
2ANQ X-ray 2.13 A 1-159 [» ]
2D0K X-ray 1.90 A/B 2-159 [» ]
2DRC X-ray 1.90 A/B 1-159 [» ]
2INQ neutron diffraction 2.20 A/B 1-159 [» ]
3DAU X-ray 1.50 A 1-159 [» ]
3DRC X-ray 1.90 A/B 1-159 [» ]
3K74 X-ray 1.95 A 1-159 [» ]
3KFY X-ray 2.08 A 1-159 [» ]
3OCH X-ray 1.79 A/B 1-159 [» ]
3QL3 X-ray 1.80 A 1-159 [» ]
3QYL X-ray 1.79 A 1-159 [» ]
3QYO X-ray 2.09 A 1-159 [» ]
3R33 X-ray 2.09 A 1-159 [» ]
4DFR X-ray 1.70 A/B 1-159 [» ]
4EIG X-ray 2.50 A 1-159 [» ]
4EIZ X-ray 2.20 A/B 1-159 [» ]
4EJ1 X-ray 1.75 A/B 1-159 [» ]
4FHB X-ray 2.80 A 1-159 [» ]
4GH8 X-ray 1.85 A/B 1-158 [» ]
4I13 X-ray 1.60 A 1-159 [» ]
4I1N X-ray 1.89 A 1-159 [» ]
4KJJ X-ray 1.15 A 1-159 [» ]
4KJK X-ray 1.35 A 1-159 [» ]
4KJL X-ray 1.38 A 1-159 [» ]
4NX6 X-ray 1.35 A 1-159 [» ]
4NX7 X-ray 1.15 A 1-159 [» ]
5DFR X-ray 2.30 A 1-159 [» ]
6DFR X-ray 2.40 A 1-159 [» ]
7DFR X-ray 2.50 A 1-159 [» ]
DisProti DP00301.
ProteinModelPortali P0ABQ4.
SMRi P0ABQ4. Positions 1-159.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35824N.
IntActi P0ABQ4. 16 interactions.
MINTi MINT-1239602.
STRINGi 511145.b0048.

Chemistry

BindingDBi P0ABQ4.
ChEMBLi CHEMBL2364669.

2D gel databases

SWISS-2DPAGE P0ABQ4.

Proteomic databases

PaxDbi P0ABQ4.
PRIDEi P0ABQ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73159 ; AAC73159 ; b0048 .
BAB96616 ; BAB96616 ; BAB96616 .
GeneIDi 12933205.
944790.
KEGGi ecj:Y75_p0048.
eco:b0048.
PATRICi 32115195. VBIEscCol129921_0049.

Organism-specific databases

EchoBASEi EB0322.
EcoGenei EG10326. folA.

Phylogenomic databases

eggNOGi COG0262.
HOGENOMi HOG000040233.
InParanoidi P0ABQ4.
KOi K00287.
OMAi CITHVEA.
OrthoDBi EOG6KT2V2.
PhylomeDBi P0ABQ4.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .
BioCyci EcoCyc:DIHYDROFOLATEREDUCT-MONOMER.
ECOL316407:JW0047-MONOMER.
MetaCyc:DIHYDROFOLATEREDUCT-MONOMER.
SABIO-RK P0ABQ4.

Miscellaneous databases

EvolutionaryTracei P0ABQ4.
PROi P0ABQ4.

Gene expression databases

Genevestigatori P0ABQ4.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000194. DHFR. 1 hit.
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The amino-acid sequence of the dihydrofolate reductase of a trimethoprim-resistant strain of Escherichia coli."
    Stone D., Phillips A.W., Burchall J.J.
    Eur. J. Biochem. 72:613-624(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOZYME 1).
    Strain: B [RT500].
  2. "Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli."
    Bennett C.D., Rodkey J.A., Sondey J.M., Hirschmann R.
    Biochemistry 17:1328-1337(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: B [MB1428].
  3. "Nucleotide sequence of the E coli gene coding for dihydrofolate reductase."
    Smith D.R., Calvo J.M.
    Nucleic Acids Res. 8:2255-2274(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding."
    Baccanari D.P., Stone D., Kuyper L.
    J. Biol. Chem. 256:1738-1747(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOZYME 2).
    Strain: B [RT500].
  5. "Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim."
    Flensburg J., Skoeld O.
    Eur. J. Biochem. 162:473-476(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1810.
  6. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "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."
    Filman D.J., Bolin J.T., Matthews D.A., Kraut J.
    J. Biol. Chem. 257:13663-13672(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  11. "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."
    Bystroff C., Oatley S.J., Kraut J.
    Biochemistry 29:3263-3277(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  12. "Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding."
    Bystroff C., Kraut J.
    Biochemistry 30:2227-2239(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  13. "Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications."
    Reyes V.M., Sawaya M.R., Brown K.A., Kraut J.
    Biochemistry 34:2710-2723(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH NADPH; FOLATE; 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE.
  14. "Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4."
    Lee H., Reyes V.M., Kraut J.
    Biochemistry 35:7012-7020(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH 5-FORMYLTETRAHYDROFOLATE.
  15. "Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence."
    Sawaya M.R., Kraut J.
    Biochemistry 36:586-603(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH NADPH; METHOTREXATE AND TETRAHYDROFOLATE.
  16. "Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase."
    Iwakura M., Maki K., Takahashi H., Takenawa T., Yokota A., Katayanagi K., Kamiyama T., Gekko K.
    J. Biol. Chem. 281:13234-13246(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FOLATE, CATALYTIC ACTIVITY, MUTAGENESIS OF MET-16; MET-20; MET-42; CYS-85; MET-92 AND CYS-152, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "A 2.13 A structure of E. coli dihydrofolate reductase bound to a novel competitive inhibitor reveals a new binding surface involving the M20 loop region."
    Summerfield R.L., Daigle D.M., Mayer S., Mallik D., Hughes D.W., Jackson S.G., Sulek M., Organ M.G., Brown E.D., Junop M.S.
    J. Med. Chem. 49:6977-6986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
  18. "Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate."
    Bennett B., Langan P., Coates L., Mustyakimov M., Schoenborn B., Howell E.E., Dealwis C.
    Proc. Natl. Acad. Sci. U.S.A. 103:18493-18498(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NEUTRON DIFFRACTION (2.20 ANGSTROMS) IN COMPLEX WITH METHOTREXATE.
  19. "X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design."
    Bennett B.C., Wan Q., Ahmad M.F., Langan P., Dealwis C.G.
    J. Struct. Biol. 166:162-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH METHOTREXATE AND NADPH.

Entry informationi

Entry nameiDYR_ECOLI
AccessioniPrimary (citable) accession number: P0ABQ4
Secondary accession number(s): P00379
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The strain K12 sequence is shown.
Strain B [RT500] is resistant to 500 micrograms per milliliter of trimethoprim.
Strain B [MB1428] is methotrexate-resistant.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3