Conformation of ATP and ADP bound to N10-formyltetrahydrofolate synthetase determined by TRNOE NMR spectroscopy.
Conformation of ATP and ADP bound to N10-formyltetrahydrofolate synthetase determined by TRNOE NMR spectroscopy.
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通过 TRNOE NMR 光谱测定与 N10-甲酰四氢叶酸合成酶结合的 ATP 和 ADP 的构象。
DOI：
10.1021/bi00169a010
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Himes,RH
中科院分区：
文献类型：
--
作者：
Song,S;VanderVelde,D;Gunn,CW;Himes,RH
Revised Manuscript Received November 5, 1993® abstract: ATP and ADP bind to N10-CHO-H4folate synthetase from Clostridium cylindrosporum at four identical sites. Although both ADP and ATP bind to the enzyme with essentially the same Ka values as the Mg2+-nucleotide complexes, only the Mg2+* nucleotides are kinetically active. Using transferred nuclear Overhauser effect (TRNOE) NMR spectroscopy, we have measured the time-dependent NOE buildup rates of selected protons in ADP and ATP bound to N10-CHO-H4folate synthetase afterpreirradiating protons HU, H2', H3\and H4'. The results were used to calculate interproton distances. In order to define the conformations of ADP and ATP bound to the enzyme, we used the TRNOE distance constraints in a distance geometry algorithm. The results of the distance geometry calculations suggest that, within experimental error, the conformations of both ADP and ATP (with or without Mg2+) have an average glycosidic torsion angle X (04/-Cl/-N9-C8) of 100±20 and a sugar pucker angle'F'(C5/-C4/-C3'-03') of 85±5. These values are consistent modeling after energy minimization, which has X= CV-endo conformation.
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影响因子：
4.8
作者：
N. Curthoys;J. Rabinowitz
通讯作者：
J. Rabinowitz
肝素-琼脂糖色谱法利用酶纯化四氢叶酸：C1-四氢叶酸合成酶和10-甲酰四氢叶酸合成酶。
影响因子：
2.9
作者：
C. Staben;T. Whitehead;J. Rabinowitz
通讯作者：
J. Rabinowitz
通过核奥弗豪瑟效应研究配体构象和配体-酶相互作用。
影响因子：
--
作者：
P. Rosevear;A. Mildvan
通讯作者：
A. Mildvan
影响因子：
2.9
作者：
N. Curthoys;L. D'Ari Straus;J. Rabinowitz
通讯作者：
J. Rabinowitz
游离并与牛心蛋白激酶结合的四氨钴 (III)-腺苷 5-三磷酸构象的核奥弗豪瑟效应研究。
影响因子：
2.9
作者：
Rosevear,PR;Bramson,HN;O'Brian,C;Kaiser,ET;Mildvan,AS
通讯作者：
Mildvan,AS