摘要
We have employed 15N NMR to characterize the conformations of Escherichia coli dihydrofolate reductase (ECDHFR) in complex with [5-15N]folate or [5-15N]methotrexate (MTX). Two 15N resonances were observed for DHFR/MTX binary complex. The relative population of these two conformations is pH dependent. Addition of NADP+ or NADPH results in the disappearance of the low field resonance. In contrast, only one conformation was observed for both the DHFR/folate and DHFR/folate/NADP+ complexes. However, the 15N chemical shift of [5-15N]folate in the binary DHFR/folate complex is 7.28 ppm upfield from that of the ternary complex, suggesting the possible loss of a hydrogen bonding to N5 of folate in the ternary complex.
原文 | 英語 |
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頁(從 - 到) | 231-234 |
頁數 | 4 |
期刊 | FEBS Letters |
卷 | 289 |
發行號 | 2 |
DOIs | |
出版狀態 | 已發佈 - 1991 9月 9 |
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