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Challenging the limit: NMR assignment of a 31 kDa helical membrane protein.

ABSTRACT: 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.

SUBMITTER: Huang C

PROVIDER: S-EPMC2862971 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Challenging the limit: NMR assignment of a 31 kDa helical membrane protein.

Huang Chengdong C Mohanty Smita S

Journal of the American Chemical Society 20100301 11

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 prot ...[more]

PMID: 20178386

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