5WPW

Crystal structure of coconut allergen cocosin

Summary for 5WPW

• Entry DOI: 10.2210/pdb5wpw/pdb
• Descriptor: 11S globulin isoform 1 (2 entities in total)
• Functional Keywords: 11s globulin, seed storage protein, allergen
• Biological source: Cocos nucifera (Coconut palm)
• Total number of polymer chains: 2
• Total formula weight: 96356.53

Authors

Jin, T.,Zhang, Y. (deposition date: 2016-11-21, release date: 2017-10-25, Last modification date: 2024-10-23)

Primary citation

Jin, T.,Wang, C.,Zhang, C.,Wang, Y.,Chen, Y.W.,Guo, F.,Howard, A.,Cao, M.J.,Fu, T.J.,McHugh, T.H.,Zhang, Y.
Crystal Structure of Cocosin, A Potential Food Allergen from Coconut (Cocos nucifera)
J. Agric. Food Chem., 65:7560-7568, 2017

PubMed 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.

PubMed: 28712292
DOI: 10.1021/acs.jafc.7b02252

Experimental method

X-RAY DIFFRACTION (1.847 Å)