5XBD

Disulfide-constrained Wound Healing Peptide Derived from Pereskia bleo

Summary for 5XBD

• Entry DOI: 10.2210/pdb5xbd/pdb
• NMR Information: BMRB: 36066
• Descriptor: pB1 (1 entity in total)
• Functional Keywords: disulfide bond, pereskia bleo, cystein-rich peptide crp, anti-microbial peptide, unknown function
• Biological source: Pereskia bleo
• Total number of polymer chains: 1
• Total formula weight: 3838.44

Authors

Xiao, T.,Tam, J.P. (deposition date: 2017-03-17, release date: 2018-02-14, Last modification date: 2024-10-23)

Primary citation

Loo, S.,Kam, A.,Xiao, T.,Tam, J.P.
Bleogens: Cactus-Derived Anti-Candida Cysteine-Rich Peptides with Three Different Precursor Arrangements
Front Plant Sci, 8:2162-2162, 2017

PubMed Abstract: Cysteine-rich peptides (CRPs) play important host-defense roles in plants. However, information concerning CRPs in the Cactaceae (cactus) family is limited, with only a single cactus-derived CRP described to date. Here, we report the identification of 15 novel CRPs with three different precursor architectures, bleogens pB1-15 from of the Cactaceae family. By combining proteomic and transcriptomic methods, we showed that the prototype, bleogen pB1, contained 36 amino acid residues, a six-cysteine motif typical of the six-cysteine-hevein-like peptide (6C-HLP) family, and a type I two-domain precursor consisting of an endoplasmic reticulum (ER) and a mature domain. In contrast, the precursors of the other 14 bleogens contained a type II three-domain architecture with a propeptide domain inserted between the ER and the mature bleogen domain. Four of these 14 bleogens display a third type of architecture with a tandemly repeating bleogen domain. A search of the Onekp database revealed that <1% plant species possess three different precursor architectures for the biosynthesis of 6C-HLPs, including , and sp. NMR analysis confirmed that bleogen pB1 has cystine-knot disulfide connectivity as well as a two-beta-sheet and a four-loop structural fold that is similar to other 6C-HLPs. Sequence analysis, structural studies, and modeling revealed that bleogen pB1 has a cation-polar-cation motif, a signature heparin-binding motif that was confirmed by heparin affinity chromatography. Cell-based assays showed that bleogen pB1 is non-toxic to mammalian cells but functions as an anti-Candida peptide. Taken together, our findings provide insight into the occurrence, functions and precursor architectures of CRPs in the cactus family.

PubMed: 29312404
DOI: 10.3389/fpls.2017.02162

Experimental method

SOLUTION NMR