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Preliminary X‐ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein
Author(s) -
Maruyama Nobuyuki,
Goshi Tomohiro,
Sugiyama Shigeru,
Niiyama Mayumi,
Adachi Hiroaki,
Takano Kazufumi,
Murakami Satoshi,
Inoue Tsuyoshi,
Mori Yusuke,
Matsumura Hiroyoshi,
Mikami Bunzo
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14027484
Subject(s) - sorting , storage protein , protein targeting , vacuole , microbiology and biotechnology , crystallography , chemistry , biology , biochemistry , membrane protein , membrane , gene , algorithm , computer science , cytoplasm
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 P 3 1 21, with unit‐cell parameters a = b = 116.4, c = 86.1 Å.