4PMK

Crystal structure of kiwellin

Summary for 4PMK

• Entry DOI: 10.2210/pdb4pmk/pdb
• Descriptor: Kiwellin, CHLORIDE ION (3 entities in total)
• Functional Keywords: double psi beta barrel, plant protein
• Biological source: Actinidia chinensis (Kiwi)
• Total number of polymer chains: 2
• Total formula weight: 39612.54

Authors

Hamiaux, C.,Baker, E.N.,Atkinson, R.G. (deposition date: 2014-05-22, release date: 2014-08-13, Last modification date: 2024-10-30)

Primary citation

Hamiaux, C.,Maddumage, R.,Middleditch, M.J.,Prakash, R.,Brummell, D.A.,Baker, E.N.,Atkinson, R.G.
Crystal structure of kiwellin, a major cell-wall protein from kiwifruit.
J.Struct.Biol., 187:276-281, 2014

PubMed Abstract: Kiwellin is a cysteine-rich, cell wall-associated protein with no known structural homologues. It is one of the most abundant proteins in kiwifruit (Actinidia spp.), and has been shown to be recognised by IgE of some patients allergic to kiwifruit. Cleavage of kiwellin into an N-terminal 4 kDa peptide called kissper and a core domain called KiTH is mediated by actinidin in vitro, and isolation of the kissper peptide from green-fleshed kiwifruit extracts suggested it may result from in vivo processing of kiwellin. In solution, kissper is highly flexible and displays pore-forming activity in synthetic lipid-bilayers. We present here the 2.05 Å resolution crystal structure of full-length kiwellin, purified from its native source, Actinidia chinensis (gold-fleshed kiwifruit). The structure confirms the modularity of the protein and the intrinsic flexibility of kissper and reveals that KiTH harbours a double-psi β-barrel fold hooked to an N-terminal β hairpin. Comparisons with structurally-related proteins suggest that a deep gorge located at the protein surface forms a binding site for endogenous ligands.

PubMed: 25093947
DOI: 10.1016/j.jsb.2014.07.005

Experimental method

X-RAY DIFFRACTION (2.05 Å)