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

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

6 Scopus citations

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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10.1016/0014-5793(91)80549-I

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@article{cb760fad72704789b618237039441ec3,

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\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,

day = "20",

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

language = "English (US)",

volume = "283",

pages = "44--46",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

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TY - JOUR

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.

UR - https://www.scopus.com/pages/publications/0025757269

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U2 - 10.1016/0014-5793(91)80549-I

DO - 10.1016/0014-5793(91)80549-I

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C2 - 2037072

AN - SCOPUS:0025757269

SN - 0014-5793

VL - 283

SP - 44

EP - 46

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

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