Challenging the Limit: NMR Assignment of a 31 kDa Helical Membrane Protein

被引:13
作者
Huang, Chengdong [1 ]
Mohanty, Smita [1 ]
机构
[1] Auburn Univ, Dept Chem & Biochem, Auburn, AL 36849 USA
关键词
YEAST OLIGOSACCHARYL TRANSFERASE; SECONDARY STRUCTURE; ESCHERICHIA-COLI; SPECTROSCOPY; SUBUNIT; COMPLEX; STT3; C-13; CRYSTALLIZATION; IDENTIFICATION;
D O I
10.1021/ja100078z
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:3662 / +
页数:4
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