论文标题
无蛋白质结构 - 高度顺磁系统中的替代范式
NOE-less protein structures-an alternative paradigm in Highly Paramagnetic Systems
论文作者
论文摘要
迄今为止，通过NMR光谱测定蛋白质结构的当前范式是基于以核过度大冲突增强（NOE）的形式收集核对之间的距离限制。在某些情况下，这些已补充了其他信息源，例如顺磁松弛增强或残留的偶极耦合。在这里，我们首次在不使用NOE的情况下首次报告NMR的蛋白质结构测定。 Rhodopseu-Domonas palustris Tie-1的蛋白质PIOC是HIPIP，其中4FE4S簇是顺磁性的，并提供了用作替代距离约束的顺磁性松弛增强（PRE）。通过NOE结构约束获得的结构家族的比较与PRE和通过组合NOE和PRES获得的结构家族获得的结构家族，这表明它们之间的成对RMSD与每个家族中的精度相似，并且可比。这项工作为小型和动态的顺磁金属蛋白的结构表征奠定了基础，为在结构生物学中使用NMR开辟了新的范式。
The current paradigm for protein structure determination by NMR spectroscopy has thus far been based on collecting distance restrains between pairs of nuclei in the form of nuclear Overhauser enhancements (NOE). These, have in some circumstances been supplemented with other information sources such as paramagnetic relaxation enhancements or residual dipolar couplings. Here, we report for the first time a protein structure determination by NMR without the use of NOEs. The protein PioC from Rhodopseu-domonas palustris TIE-1 is an HIPIP where the 4Fe4S cluster is paramagnetic and provides the source of Paramagnetic Relaxation Enhancements (PRE) used as alternative distance constraints. Comparison of the family of structures obtained by NOE structural restraints, with that obtained by PRE and with the family of structures obtained by combining NOEs and PREs reveals that the pairwise RMSD between them are similar and comparable with the precision within each family. This work sets the stage for the structural characterization of small and dynamic paramagnetic metalloproteins opening a new paradigm in the use of NMR in structural biology.
