Literature DB >> 20178386

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

Chengdong Huang1, Smita Mohanty.   

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.

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Year:  2010        PMID: 20178386      PMCID: PMC2862971          DOI: 10.1021/ja100078z

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  26 in total

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