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The conformations of trimethoprim/ E. coli dihydrofolate reductase complexes A 15 N and 31 P NMR study
Author(s) -
Huang Fu-yung,
Yang Qing-Xian,
Huang Tai-huang,
Gelbaum Leslie,
Kuyper Lee F.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80549-i
Subject(s) - dihydrofolate reductase , ternary complex , chemistry , ternary operation , stereochemistry , nuclear magnetic resonance spectroscopy , nmr spectra database , escherichia coli , trimethoprim , crystallography , enzyme , biochemistry , spectral line , physics , antibiotics , computer science , programming language , astronomy , gene
We have employed 15 N and 31 P 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 15 N and 31 P 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.