Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama 36849, USA.
J Am Chem Soc. 2010 Mar 24;132(11):3662-3. doi: 10.1021/ja100078z.
Structural determination of membrane proteins by NMR spectroscopy remains a challenge, especially for helical membrane proteins. Here we report the NMR assignment and secondary structure of a 31 kDa helical membrane protein, the C-terminal domain of Stt3p. The C-terminal domain of Stt3p has been proposed to be the catalytic domain of yeast oligosaccharyl transferase (OT), a multisubunit membrane-associated enzyme complex catalyzing N-glycosylation, which is an essential and highly conserved protein modification. NMR assignment is the first critical step in the determination of the high-resolution solution structure and further structure-function studies.
通过 NMR 光谱法确定膜蛋白的结构仍然具有挑战性，尤其是对于螺旋膜蛋白。在这里，我们报告了一种 31 kDa 螺旋膜蛋白，Stt3p 的 C 末端结构域的 NMR 结构测定和二级结构。Stt3p 的 C 末端结构域被认为是酵母寡糖基转移酶（OT）的催化结构域，OT 是一种多亚基膜相关酶复合物，催化 N-糖基化，这是一种必不可少且高度保守的蛋白质修饰。NMR 结构测定是确定高分辨率溶液结构和进一步结构功能研究的关键的第一步。
