Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex

Shovanlal Gayen; CongBao Kang

doi:10.1016/j.bbrc.2011.05.050

Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex

Biochem Biophys Res Commun. 2011 Jun 10;409(3):572-6. doi: 10.1016/j.bbrc.2011.05.050. Epub 2011 May 15.

Authors

Shovanlal Gayen¹, CongBao Kang

Affiliation

¹ Experimental Therapeutics Center, The Agency for Science, Technology and Research, Singapore 138669, Singapore.

PMID: 21609714
DOI: 10.1016/j.bbrc.2011.05.050

Abstract

Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein. Human Ost4 is a small membrane protein and belongs to one of the seven subunits of human OST. This study determined the solution structure of human Ost4 in solvent system using NMR spectroscopy. Ost4 was demonstrated that the residues 5-30 adopt an α-helical structure. A kink structure was observed in the transmembrane domain, which may be important for its function.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Hexosyltransferases / chemistry*
Humans
Membrane Proteins / chemistry*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits / chemistry
Solutions

Substances

Membrane Proteins
Protein Subunits
Solutions
Hexosyltransferases
dolichyl-diphosphooligosaccharide - protein glycotransferase