2LAT

Solution structure of a Human minimembrane protein OST4

Summary for 2LAT

Entry DOI	10.2210/pdb2lat/pdb
NMR Information	BMRB: 17537
Descriptor	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 (1 entity in total)
Functional Keywords	membrane protein, oligosaccharyltransferase, integral membrane protein
Biological source	Homo sapiens (human)
Cellular location	Membrane; Single-pass membrane protein (Potential): P0C6T2
Total number of polymer chains	1
Total formula weight	4196.00
Authors	Gayen, S.,Kang, C. (deposition date: 2011-03-21, release date: 2011-06-29, Last modification date: 2024-05-15)
Primary citation	Gayen, S.,Kang, C. Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex. Biochem.Biophys.Res.Commun., 409:572-576, 2011 Cited by PubMed 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. PubMed: 21609714 DOI: 10.1016/j.bbrc.2011.05.050 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation