Structural highlights
Function
[DEF1_PETHY] Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds.,Janssen BJ, Schirra HJ, Lay FT, Anderson MA, Craik DJ Biochemistry. 2003 Jul 15;42(27):8214-22. PMID:12846570[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Janssen BJ, Schirra HJ, Lay FT, Anderson MA, Craik DJ. Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds. Biochemistry. 2003 Jul 15;42(27):8214-22. PMID:12846570 doi:10.1021/bi034379o
