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. 2003 Jul 15;42(27):8214-22.
doi: 10.1021/bi034379o.

Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds

Bert J C Janssen  1 , Horst Joachim Schirra, Fung T Lay, Marilyn A Anderson, David J Craik
Affiliations

Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds

Bert J C Janssen et al. Biochemistry. .

Abstract

The structure of a novel plant defensin isolated from the flowers of Petunia hybrida has been determined by (1)H NMR spectroscopy. P. hybrida defensin 1 (PhD1) is a basic, cysteine-rich, antifungal protein of 47 residues and is the first example of a new subclass of plant defensins with five disulfide bonds whose structure has been determined. PhD1 has the fold of the cysteine-stabilized alphabeta motif, consisting of an alpha-helix and a triple-stranded antiparallel beta-sheet, except that it contains a fifth disulfide bond from the first loop to the alpha-helix. The additional disulfide bond is accommodated in PhD1 without any alteration of its tertiary structure with respect to other plant defensins. Comparison of its structure with those of classic, four-disulfide defensins has allowed us to identify a previously unrecognized hydrogen bond network that is integral to structure stabilization in the family.

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