4X9U

Crystal structure of the kiwifruit allergen Act d 5

Summary for 4X9U

• Entry DOI: 10.2210/pdb4x9u/pdb
• Descriptor: Kiwellin (2 entities in total)
• Functional Keywords: allergen, plant protein
• Biological source: Actinidia deliciosa (Kiwi)
• Cellular location: Secreted : P84527
• Total number of polymer chains: 2
• Total formula weight: 39833.89

Authors

Offermann, L.R.,Perdue, M.L.,Giangrieco, I.,Tamburrini, M.,Ciardiello, M.A.,Chruszcz, M. (deposition date: 2014-12-11, release date: 2015-07-29, Last modification date: 2023-11-15)

Primary citation

Offermann, L.R.,Giangrieco, I.,Perdue, M.L.,Zuzzi, S.,Santoro, M.,Tamburrini, M.,Cosgrove, D.J.,Mari, A.,Ciardiello, M.A.,Chruszcz, M.
Elusive Structural, Functional, and Immunological Features of Act d 5, the Green Kiwifruit Kiwellin.
J.Agric.Food Chem., 63:6567-6576, 2015

PubMed Abstract: Kiwellin (Act d 5) is an allergenic protein contained in kiwifruit pulp in high amounts. The aim of this study was to investigate the three-dimensional structure of the natural molecule from green kiwifruit and its possible function. Kiwellin was crystallized, and its structure, including post-translational modifications, was elucidated. The molecular weight and structural features, in solution, were analyzed by gel filtration and circular dichroism, respectively. Although structurally similar to expansin, kiwellin lacks expansin activity and carbohydrate binding. A specific algorithm was applied to investigate any possible IgE reactivity correlation between kiwellin and a panel of 102 allergens, including expansins and other carbohydrate-binding allergens. The available data suggest a strong dependence of the kiwellin structure on the environmental/experimental conditions. This dependence therefore poses challenges in detecting the correlations between structural, functional, and immunological features of this protein.

PubMed: 26146952
DOI: 10.1021/acs.jafc.5b02159

Experimental method

X-RAY DIFFRACTION (2.1 Å)