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dhfr dihydrofolate reductase [ Escherichia coli ]

Gene ID: 13906554, discontinued on 16-Jul-2020
  • This record was discontinued.
Gene symbol
dhfr
Gene description
dihydrofolate reductase
Locus tag
D616_p72001
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli (strain: 5509)
Lineage
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
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Location:
plasmid: pZS50
Sequence:
NC_019082.1 (4613..5110)
Genomic Sequence:
NC_019082.1

Go to nucleotide: Graphics FASTA GenBank

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Homologous residues were found to be conserved when comparing human and Escherichia coli dihydrofolate reductase structures.
    Title: Evolution Conserves the Network of Coupled Residues in Dihydrofolate Reductase.
  2. A high-pressure crystallographic study was conducted on Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP(+) in crystal forms containing both the open and closed conformations of the M20 loop under high-pressure conditions of up to 800 MPa. At pressures between 270 and 500 MPa the crystal form containing the open conformation exhibited a phase transition from P21 to C2.
    Title: High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP().
  3. Data suggest that conformation of the Met-20 loop of DHFR has a dramatic effect on the ordering of active site hydration; DHFR active site exhibits a strong correlation between substrate/dihydrofolate N5 position basicity and conformation of the Met-20 loop.
    Title: The role of the Met(20) loop in the hydride transfer in Escherichia coli dihydrofolate reductase.
  4. The orthologous inter-species replacements caused a marked drop (in the range 10-90%) in bacterial growth rate despite the fact that most orthologous DHFRs are as stable as E.coli DHFR at 37 degrees C and are more catalytically active than E. coli DHFR.
    Title: Protein Homeostasis Imposes a Barrier on Functional Integration of Horizontally Transferred Genes in Bacteria.
  5. Binary and ternary complexes of DHFR containing cofactor NADPH, inhibitor methotrexate (MTX), or both NADPH and MTX were characterized by 193 nm ultraviolet photodissociation (UVPD) mass spectrometry.
    Title: Structural Characterization of Dihydrofolate Reductase Complexes by Top-Down Ultraviolet Photodissociation Mass Spectrometry.
  6. Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway
    Title: Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.
  7. Fast (femtosecond to picosecond) protein motions in DHFR are not coupled to hydride transfer and provides an integrative computational and experimental approach to resolve fast dynamics coupled to chemical steps in enzyme catalysis.
    Title: Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies.
  8. The disorder and/or dynamics associated with bound dihydrofolate likely arises due to the 222 symmetry associated with the R67 active site in dihydrofolate reductase.
    Title: Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase.
  9. The human dihydrofolate reductase is relatively less stable than its E.coli counterpart.
    Title: [Comparison of Physico-chemical Aspects between E. coli and Human Dihydrofolate Reductase: an Equilibrium Unfolding Study].
  10. Data show that parallel evolution of structured and disordered dihydrofolate ( reductases afforded comparable increases in activity without substantially changing the dynamic properties of the starting scaffolds.
    Title: Comparative laboratory evolution of ordered and disordered enzymes.
Submit: New GeneRIF Correction See all GeneRIFs (12)
Preferred Names
dihydrofolate reductase

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_019082.1 Reference assembly

    Range
    4613..5110
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_006953616.1 dihydrofolate reductase [Escherichia coli]

    Status: PROVISIONAL

Nucleotide Protein
Heading Accession and Version

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