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

FEBS Letters

Huang, Tai-huang¹  Kuyper, Lee F.³  Gelbaum, Leslie²  Huang, Fu-yung¹  Yang, Qing-Xian¹ 

[1] School of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA;Research Center for Biotechnology, Georgia Institute of Technology, Atlanta, GA 30332, USA;Burroughs Wellcome Co., Research Triangle Park, NC 27709, USA

关键词: Dihydrofolate reductase;    E. coli;    Trimethoprim;    Conformation;    NMR;    15N;    31P;    NADP+;   

DOI  :  10.1016/0014-5793(91)80549-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown