4pmk | pdb_00004pmk

Crystal structure of kiwellin

spinqualitylabelsall models 4pmk, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pmk is a 2 chain structure with sequence from Actinidia chinensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 4kDa 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 2.05A 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 beta-barrel fold hooked to an N-terminal beta hairpin. Comparisons with structurally-related proteins suggest that a deep gorge located at the protein surface forms a binding site for endogenous ligands. Crystal structure of kiwellin, a major cell-wall protein from kiwifruit.,Hamiaux C, Maddumage R, Middleditch MJ, Prakash R, Brummell DA, Baker EN, Atkinson RG J Struct Biol. 2014 Aug 2. pii: S1047-8477(14)00163-4. doi:, 10.1016/j.jsb.2014.07.005. PMID:25093947 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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