FEBS Letters | |
The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study | |
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
【 预 览 】
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