7L53
Solution NMR structure of the monomeric form of the cyclic plant protein PDP-23 in CD3CN/H2O
Summary for 7L53
Entry DOI | 10.2210/pdb7l53/pdb |
Related | 7L51 7L54 7L55 |
NMR Information | BMRB: 30828 |
Descriptor | Cyclic plant protein PDP-23 (1 entity in total) |
Functional Keywords | macrocyclic peptide, hydrophobic core, plant protein |
Biological source | Zinnia elegans |
Total number of polymer chains | 1 |
Total formula weight | 3135.51 |
Authors | Payne, C.D.,Rosengren, K.J. (deposition date: 2020-12-21, release date: 2021-01-20, Last modification date: 2023-06-14) |
Primary citation | Payne, C.D.,Franke, B.,Fisher, M.F.,Hajiaghaalipour, F.,McAleese, C.E.,Song, A.,Eliasson, C.,Zhang, J.,Jayasena, A.S.,Vadlamani, G.,Clark, R.J.,Minchin, R.F.,Mylne, J.S.,Rosengren, K.J. A chameleonic macrocyclic peptide with drug delivery applications. Chem Sci, 12:6670-6683, 2021 Cited by PubMed Abstract: Head-to-tail cyclized peptides are intriguing natural products with unusual properties. The PawS-Derived Peptides (PDPs) are ribosomally synthesized as part of precursors for seed storage albumins in species of the daisy family, and are post-translationally excised and cyclized during proteolytic processing. Here we report a PDP twice the typical size and with two disulfide bonds, identified from seeds of . In water, synthetic PDP-23 forms a unique dimeric structure in which two monomers containing two β-hairpins cross-clasp and enclose a hydrophobic core, creating a square prism. This dimer can be split by addition of micelles or organic solvent and in monomeric form PDP-23 adopts open or closed V-shapes, exposing different levels of hydrophobicity dependent on conditions. This chameleonic character is unusual for disulfide-rich peptides and engenders PDP-23 with potential for cell delivery and accessing novel targets. We demonstrate this by conjugating a rhodamine dye to PDP-23, creating a stable, cell-penetrating inhibitor of the P-glycoprotein drug efflux pump. PubMed: 34040741DOI: 10.1039/d1sc00692d PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report