15N NMR studies of the conformation of E. coli dihydrofolate reductase in complex with folate or methotrexate

Fu Yung Huang, Qing Xian Yang, Tai huang Huang

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We have employed 15N NMR to characterize the conformations of Escherichia coli dihydrofolate reductase (ECDHFR) in complex with [5-15N]folate or [5-15N]methotrexate (MTX). Two 15N resonances were observed for DHFR/MTX binary complex. The relative population of these two conformations is pH dependent. Addition of NADP+ or NADPH results in the disappearance of the low field resonance. In contrast, only one conformation was observed for both the DHFR/folate and DHFR/folate/NADP+ complexes. However, the 15N chemical shift of [5-15N]folate in the binary DHFR/folate complex is 7.28 ppm upfield from that of the ternary complex, suggesting the possible loss of a hydrogen bonding to N5 of folate in the ternary complex.

Original languageEnglish
Pages (from-to)231-234
Number of pages4
JournalFEBS Letters
Volume289
Issue number2
DOIs
Publication statusPublished - 1991 Sep 9

Fingerprint

Tetrahydrofolate Dehydrogenase
Folic Acid
Methotrexate
Escherichia coli
Conformations
Nuclear magnetic resonance
NADP
Chemical shift
Hydrogen Bonding
Hydrogen bonds
Population

Keywords

  • Dihydrofolate reductase
  • Folate
  • Methotrexate
  • NADP
  • NMR

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

15N NMR studies of the conformation of E. coli dihydrofolate reductase in complex with folate or methotrexate. / Huang, Fu Yung; Yang, Qing Xian; Huang, Tai huang.

In: FEBS Letters, Vol. 289, No. 2, 09.09.1991, p. 231-234.

Research output: Contribution to journalArticle

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