The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study

Fu yung Huang; Qing Xian Yang; Tai huang Huang; Leslie Gelbaum; Lee F. Kuyper

doi:10.1016/0014-5793(91)80549-I

The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A ¹⁵N and ³¹P NMR study

Fu yung Huang
, Qing Xian Yang
, Tai huang Huang^*
, Leslie Gelbaum
, Lee F. Kuyper

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

We have employed ¹⁵N and ³¹P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP⁺. A single conformation was observed for TMP/DHFR, NADP⁺/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP⁺/DHFR both the ¹⁵N and ³¹P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP⁺ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.

Original language	English
Pages (from-to)	44-46
Number of pages	3
Journal	FEBS Letters
Volume	283
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(91)80549-I
Publication status	Published - 1991 May 20
Externally published	Yes

Keywords

Conformation
Dihydrofolate reductase
E. coli
NMR, N, P, NADP
Trimethoprim

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(91)80549-I

Cite this

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title = "The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study",

abstract = "We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.",

keywords = "Conformation, Dihydrofolate reductase, E. coli, NMR, N, P, NADP, Trimethoprim",

author = "Huang, \{Fu yung\} and Yang, \{Qing Xian\} and Huang, \{Tai huang\} and Leslie Gelbaum and Kuyper, \{Lee F.\}",

note = "Funding Information: Acknowledgemems: We wish to thank Dr, E. Howell of University of Tennessc for lh¢ l\textbackslash{}]¢rllrotl\textasciitilde{}g ill of{"} lh\textasciitilde{} DHFR over.praducing E, col/ strain. Technical assistancc.,so f M\textasciitilde{}. L.E. Khaw is \textasciitilde{}¢knowlcdlt,¢d, This work is supported by Grant GM-39779 from Natlonal lnstitul¢ of Health.",

year = "1991",

month = may,

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doi = "10.1016/0014-5793(91)80549-I",

language = "English",

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T1 - The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study

AU - Huang, Fu yung

AU - Yang, Qing Xian

AU - Huang, Tai huang

AU - Gelbaum, Leslie

AU - Kuyper, Lee F.

N1 - Funding Information: Acknowledgemems: We wish to thank Dr, E. Howell of University of Tennessc for lh¢ l\]¢rllrotl~g ill of" lh~ DHFR over.praducing E, col/ strain. Technical assistancc.,so f M~. L.E. Khaw is ~¢knowlcdlt,¢d, This work is supported by Grant GM-39779 from Natlonal lnstitul¢ of Health.

PY - 1991/5/20

Y1 - 1991/5/20

N2 - We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.

AB - We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.

KW - Conformation

KW - Dihydrofolate reductase

KW - E. coli

KW - NMR, N, P, NADP

KW - Trimethoprim

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