4PMK

Crystal structure of kiwellin

4PMK の概要

• エントリーDOI: 10.2210/pdb4pmk/pdb
• 分子名称: Kiwellin, CHLORIDE ION (3 entities in total)
• 機能のキーワード: double psi beta barrel, plant protein
• 由来する生物種: Actinidia chinensis (Kiwi)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39612.54

構造登録者

Hamiaux, C.,Baker, E.N.,Atkinson, R.G. (登録日: 2014-05-22, 公開日: 2014-08-13, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.05 Å)