Preliminary X-ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein

β-Conglycinin is a major seed storage protein in soybeans, which are an important source of protein. The major subunits (α, α′ and β) of β-conglycinin are sorted to protein-storage vacuoles in seed cells. Vacuolar sorting receptor (VSR) is an integral membrane protein that recognizes the sorting determinant of vacuolar proteins, including β-conglycinin, and regulates their sorting process. Vacuolar sorting determinants of the α′ and β subunits of β-conglycinin exist in their C-terminal peptides. Here, the preliminary X-ray diffraction analysis of the binding domain of soybean VSR crystallized with the peptide responsible for the sorting determinant in β-conglycinin is reported. X-ray diffraction data were collected to a resolution of 3.5 Å. The crystals belonged to space group P3121, with unit-cell parameters a = b = 116.4, c = 86.1 Å.

Source: Acta Crystallographica Section F - January 28, 2015 Category: Biochemistry Authors: Maruyama, N.Goshi, T.Sugiyama, S.Niiyama, M.Adachi, H.Takano, K.Murakami, S.Inoue, T.Mori, Y.Matsumura, H.Mikami, B. Tags: soybean seed storage protein β -conglycinin vacuolar sorting receptor research communications Source Type: research