Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
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DOI：
10.1007/s10858-014-9882-7
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发表时间：
2015-01-01
影响因子：
2.7
通讯作者：
Kojima, Chojiro
中科院分区：
文献类型：
--
作者：
Furuita, Kyoko;Kataoka, Saori;Kojima, Chojiro
可溶性蛋白质的核磁共振结构测定在很大程度上取决于NOE产生的距离限制。在这项研究中，我们研究了顺磁驰豫增强(Pre)衍生的距离约束对蛋白质结构确定的影响。由于NOE限制数目不足，传统的NOE方法不能确定富含环的可溶性蛋白SIN1的高分辨结构。通过使用基于NOE的结构确定过程中得到的867个预导出的距离约束，可以成功地确定SIN1的高分辨率结构。通过增加预导出距离约束的数目，提高了所确定结构的收敛和精度。这项研究表明，当NOE约束的数量不足时，预导出的距离约束在确定可溶蛋白质的高分辨率结构中是有用的。
NMR structure determination of soluble proteins depends in large part on distance restraints derived from NOE. In this study, we examined the impact of paramagnetic relaxation enhancement (PRE)-derived distance restraints on protein structure determination. A high-resolution structure of the loop-rich soluble protein Sin1 could not be determined by conventional NOE-based procedures due to an insufficient number of NOE restraints. By using the 867 PRE-derived distance restraints obtained from the NOE-based structure determination procedure, a high-resolution structure of Sin1 could be successfully determined. The convergence and accuracy of the determined structure were improved by increasing the number of PRE-derived distance restraints. This study demonstrates that PRE-derived distance restraints are useful in the determination of a high-resolution structure of a soluble protein when the number of NOE constraints is insufficient.