1UIJ

Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)

1UIJ の概要

• エントリーDOI: 10.2210/pdb1uij/pdb
• 関連するPDBエントリー: 1UIK
• 分子名称: beta subunit of beta conglycinin (2 entities in total)
• 機能のキーワード: double-stranded beta helix, seed storage protein, sugar binding protein
• 由来する生物種: Glycine max (soybean)
• 細胞内の位置: Vacuole, aleurone grain: P25974
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 288651.37

構造登録者

Maruyama, N.,Maruyama, Y.,Tsuruki, T.,Okuda, E.,Yoshikawa, M.,Utsumi, S. (登録日: 2003-07-16, 公開日: 2004-07-16, 最終更新日: 2023-12-27)

主引用文献

Maruyama, N.,Maruyama, Y.,Tsuruki, T.,Okuda, E.,Yoshikawa, M.,Utsumi, S.
Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity
BIOCHIM.BIOPHYS.ACTA, 1648:99-104, 2003

PubMed Abstract: beta-Conglycinin is composed of three kinds of subunit: alpha, alpha' and beta. A phagocytosis-stimulating peptide sequence (MITLAIPVNKPGR), soymetide, exists in the alpha' subunit of beta-conglycinin. Met at N terminus of the soymetide is essential for the activity. When Thr at the third residue from N terminus of the soymetide is replaced by Phe or Trp, the phagocytosis-stimulating activity greatly increases (ThrMet, Lys-->Thr, Phe, or Trp) into the beta subunit after confirmation of the effects of residue replacements by molecular modeling, suggesting that the introduced mutations might not prevent the correct folding. The studies of circular dichroism (CD), gel filtration and differential scanning calorimetry (DSC) of the mutants (I122M/K124T, I122M/K124F, I122M/K124W) expressed in E. coli demonstrated that they folded and self-assembled similarly to the wild type. This was confirmed by X-ray analysis of I122M/K124W crystal where the biggest residue tryptophane was introduced. The three mutants exhibited phagocytosis activities after digestion by trypsin, and the order was the wild typePubMed: 12758152
DOI: 10.1016/S1570-9639(03)00113-4

実験手法

X-RAY DIFFRACTION (2.5 Å)