Literature DB >> 28712292

Crystal Structure of Cocosin, A Potential Food Allergen from Coconut (Cocos nucifera).

Tengchuan Jin1,2,3, Cheng Wang1,3, Caiying Zhang1, Yang Wang2, Yu-Wei Chen2, Feng Guo2, Andrew Howard2, Min-Jie Cao3, Tong-Jen Fu4, Tara H McHugh5, Yuzhu Zhang2,5.   

Abstract

Coconut (Cocos nucifera) is an important palm tree. Coconut fruit is widely consumed. The most abundant storage protein in coconut fruit is cocosin (a likely food allergen), which belongs to the 11S globulin family. Cocosin was crystallized near a century ago, but its structure remains unknown. By optimizing crystallization conditions and cryoprotectant solutions, we were able to obtain cocosin crystals that diffracted to 1.85 Å. The cocosin gene was cloned from genomic DNA isolated from dry coconut tissue. The protein sequence deduced from the predicted cocosin coding sequence was used to guide model building and structure refinement. The structure of cocosin was determined for the first time, and it revealed a typical 11S globulin feature of a double layer doughnut-shaped hexamer.

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Keywords:  11S globulin; coconut; cocosin; food allergen; hexameric structure

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Year:  2017        PMID: 28712292     DOI: 10.1021/acs.jafc.7b02252

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  1 in total

1.  Structural basis for the formation of soy protein nanofibrils.

Authors:  Leila Josefsson; Melker Cronhamn; Malin Ekman; Hugo Widehammar; Åsa Emmer; Christofer Lendel
Journal:  RSC Adv       Date:  2019-02-21       Impact factor: 4.036

  1 in total

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