4LEJ
Crystal Structure of the Korean pine (Pinus koraiensis) vicilin
Summary for 4LEJ
| Entry DOI | 10.2210/pdb4lej/pdb |
| Descriptor | Vicilin, COPPER (II) ION, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | seed storage protein, allergen, cupin, seed storage, plant protein |
| Biological source | Pinus koraiensis (channamu) |
| Total number of polymer chains | 1 |
| Total formula weight | 46502.06 |
| Authors | Jin, T.C.,Wang, Y.,Zhang, Y.Z. (deposition date: 2013-06-25, release date: 2014-01-22, Last modification date: 2024-02-28) |
| Primary citation | Jin, T.,Wang, Y.,Chen, Y.W.,Fu, T.J.,Kothary, M.H.,McHugh, T.H.,Zhang, Y. Crystal Structure of Korean Pine ( Pinus koraiensis ) 7S Seed Storage Protein with Copper Ligands. J.Agric.Food Chem., 62:222-228, 2014 Cited by PubMed Abstract: The prevalence of food allergy has increased in recent years, and Korean pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean pine vicilin purified from raw pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean pine vicilin at 2.40 Å resolution. The overall structure of pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, including peanut and soybean. Additional studies are needed to assess whether the copper-coordinating property of vicilins has a biological function in the relevant plants. The nutritional value of this copper-coordinating protein in tree nuts and other edible seeds may be worth further investigations. PubMed: 24328105DOI: 10.1021/jf4039887 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.402 Å) |
Structure validation
Download full validation report
