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

^*此作品的通信作者

研究成果: 雜誌貢獻 › 期刊論文 › 同行評審

6 引文斯高帕斯（Scopus）

摘要

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.

原文	英語
頁（從 - 到）	44-46
頁數	3
期刊	FEBS Letters
卷	283
發行號	1
DOIs	https://doi.org/10.1016/0014-5793(91)80549-I
出版狀態	已發佈 - 1991 5月 20
對外發佈	是

ASJC Scopus subject areas

生物物理學
結構生物學
生物化學
分子生物學
遺傳學
細胞生物學

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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,

day = "20",

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

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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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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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ASJC Scopus subject areas

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