Aliphatic (1)H, (13)C and (15)N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP(+) and folate.
Aliphatic (1)H, (13)C and (15)N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP(+) and folate.
复制标题
来自嗜冷菌 Moritella profunda 与 NADP( ) 和叶酸复合物的二氢叶酸还原酶的脂肪族 (1)H、(13)C 和 (15)N 化学位移分配。
DOI：
10.1007/s12104-012-9378-x
复制
发表时间：
2013
影响因子：
0.9
通讯作者：
Loveridge EJ
中科院分区：
文献类型：
--
作者：
Loveridge EJ
用13 C/15 N同位素标记和纯化了深海细菌Moritella profunda的二氢叶酸还原酶（MpDHFR）。本文报道了MpDHFR与NADP+和叶酸复合物的1H、13 C和15 N共振归属。MpDHFR的光谱表明其构象异质性比来自大肠杆菌的密切相关的DHFR中所见的要大得多。
Dihydrofolate reductase from the deep-sea bacteriumMoritella profunda(MpDHFR) has been13C/15N isotopically labelled and purified. Here, we report the aliphatic1H,13C and15N resonance assignments of MpDHFR in complex with NADP+and folate. The spectra of MpDHFR suggest considerably greater conformational heterogeneity than is seen in the closely related DHFR fromEscherichia coli.