1UIJ

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

Summary for 1UIJ

• Entry DOI: 10.2210/pdb1uij/pdb
• Related: 1UIK
• Descriptor: beta subunit of beta conglycinin (2 entities in total)
• Functional Keywords: double-stranded beta helix, seed storage protein, sugar binding protein
• Biological source: Glycine max (soybean)
• Cellular location: Vacuole, aleurone grain: P25974
• Total number of polymer chains: 6
• Total formula weight: 288651.37

Authors

Maruyama, N.,Maruyama, Y.,Tsuruki, T.,Okuda, E.,Yoshikawa, M.,Utsumi, S. (deposition date: 2003-07-16, release date: 2004-07-16, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)