1uij

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

spinqualitylabelsall models 1uij, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uij is a 6 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLCB1_SOYBN Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 (Thr<Phe<Trp). The beta subunit does not exhibit the phagocytosis-stimulating activity because the residues corresponding to the first and third residues in the soymetide are Ile and Lys, respectively. In this study, we introduced the phagocytosis-stimulating peptide sequence (Ile-->Met, 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 type<I122M/K124T<I122M/K124F<I122M/K124W as expected. Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity.,Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:12758152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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