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

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

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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 (US)
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
State	Published - May 20 1991

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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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.",

author = "Huang, {Fu yung} and Qing Yang 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\]¢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.",

year = "1991",

month = may,

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

language = "English (US)",

volume = "283",

pages = "44--46",

journal = "FEBS Letters",

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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

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.

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VL - 283

SP - 44

EP - 46

JO - FEBS Letters

JF - FEBS Letters

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ER -

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

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