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

研究成果: 雜誌貢獻文章

10 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)231-234
頁數4
期刊FEBS Letters
289
發行號2
DOIs
出版狀態已發佈 - 1991 九月 9

    指紋

ASJC Scopus subject areas

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

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