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Crystal Structure of Cocosin, A Potential Food Allergen from Coconut (Cocos nucifera)
Author(s) -
Tengchuan Jin,
Cheng Wang,
Caiying Zhang,
Yang Wang,
Yuwei Chen,
Feng Guo,
Andrew Howard,
MinJie Cao,
TongJen Fu,
Tara H. McHugh,
Yuzhu Zhang
Publication year - 2017
Publication title -
journal of agricultural and food chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.203
H-Index - 297
eISSN - 1520-5118
pISSN - 0021-8561
DOI - 10.1021/acs.jafc.7b02252
Subject(s) - cocos nucifera , random hexamer , food allergens , storage protein , biology , genomic dna , allergen , botany , food science , gene , chemistry , horticulture , biochemistry , allergy , immunology
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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