1UD1

Crystal structure of proglycinin mutant C88S

1UD1 の概要

• エントリーDOI: 10.2210/pdb1ud1/pdb
• 関連するPDBエントリー: 1FXZ 1UCX
• 分子名称: Glycinin G1 (1 entity in total)
• 機能のキーワード: glycinin, soybean, trimer, plant protein
• 由来する生物種: Glycine max (soybean)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 160999.30

構造登録者

Utsumi, S.,Adachi, M. (登録日: 2003-04-24, 公開日: 2004-02-03, 最終更新日: 2024-10-30)

主引用文献

Adachi, M.,Okuda, E.,Kaneda, Y.,Hashimoto, A.,Shutov, A.D.,Becker, C.,Utsumi, S.
Crystal Structures and Structural Stabilities of the Disulfide Bond-Deficient Soybean Proglycinin Mutants C12G and C88S.
J.Agric.Food Chem., 51:4633-4639, 2003

PubMed Abstract: The constituent subunits of seed storage protein 11S globulin have two disulfide bonds that are common among 11S globulins from legume and nonlegume seeds. In the case of the A1aB1b subunit of soybean 11S globulin, glycinin, Cys12-Cys45 and Cys88-Cys298 are observed by X-ray crystallography. The significance of these two disulfide bonds for structural stability was investigated by mutagenesis of Cys12 to Gly and of Cys88 to Ser. The disulfide bond-deficient mutants C12G and C88S could form the correct conformations identical to that of the wild-type proglycinin except in the vicinities of the mutation sites C12 and C88 as shown by their crystal structures. Thermal stability monitored by differential scanning calorimetry of the mutants indicated that the contribution of these disulfide bonds to the thermal stability of proglycinin A1aB1b is low, although there is a small difference in the extent of the contribution between the two disulfide bonds (Cys12-Cys45 > Cys88-Cys298). The contribution of Cys88-Cys298 to the resistance of proglycinin A1aB1b to proteinase digestion is higher than that of Cys12-Cys45. Possible effects of structure on the different properties of C12G and C88S are discussed.

PubMed: 14705889
DOI: 10.1021/jf026065y

実験手法

X-RAY DIFFRACTION (3.1 Å)