无NOE的蛋白质结构--高顺磁性系统中的另一种范例
NOE-less protein structures-an alternative paradigm in Highly Paramagnetic Systems
摘要：
迄今为止，通过NMR光谱测定蛋白质结构的当前范例是基于以核奥弗豪泽增强（NOE）的形式收集核对之间的距离限制。这些，在某些情况下，补充了其他信息来源，如顺磁弛豫增强或残留偶极耦合。在这里，我们报告的第一次蛋白质结构的测定NMR没有使用NOE。来自Rhodopteri-Escherichia palustris TIE-1的蛋白质PioC是HIPIP，其中4Fe 4S簇是顺磁性的，并且提供用作替代距离约束的顺磁性弛豫增强（PRE）的来源。NOE结构约束得到的结构族与PRE得到的结构族以及NOE和PRE组合得到的结构族的比较表明，它们之间的成对RMSD相似，并且每个族内的精度相当。这项工作为小的动态顺磁性金属蛋白的结构表征奠定了基础，为核磁共振在结构生物学中的应用开辟了一个新的范例。
英文摘要：
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.
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