Mohanty Biswaranjan, Serrano Pedro, Geralt Michael, Wüthrich Kurt
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.
J Biomol NMR. 2015 Jan;61(1):83-7. doi: 10.1007/s10858-014-9878-3. Epub 2014 Nov 28.
We present the NMR structure determination of the protein NP_344798.1, which forms a CCA-adding enzyme head-domain architecture and is the first structural representative of the Pfam protein family PF06042. Its structure can now serve as a template for homology modeling of the other 785 members of this protein family. With 191 residues, NP_344798.1 is the largest single-domain protein structure determined so far with the J-UNIO protocol for automated NMR structure determination. The present work thus also shows that J-UNIO based exclusively on automated projection spectroscopy (APSY) and 3D heteronuclear-resolved [H,H]-NOESY experiments, can successfully be used to obtain high-quality NMR structures of protein domains with up to 200 residues.
我们展示了蛋白质NP_344798.1的核磁共振(NMR)结构测定结果,该蛋白质形成了一种CCA添加酶头部结构域架构,是Pfam蛋白质家族PF06042的首个结构代表。其结构现在可作为该蛋白质家族其他785个成员同源建模的模板。NP_344798.1有191个残基,是迄今为止使用J-UNIO自动NMR结构测定协议确定的最大的单结构域蛋白质结构。因此,本研究还表明,仅基于自动投影光谱(APSY)和3D异核分辨[H,H]-NOESY实验的J-UNIO,可成功用于获得多达200个残基的蛋白质结构域的高质量NMR结构。