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7L53

Solution NMR structure of the monomeric form of the cyclic plant protein PDP-23 in CD3CN/H2O

Summary for 7L53
Entry DOI10.2210/pdb7l53/pdb
Related7L51 7L54 7L55
NMR InformationBMRB: 30828
DescriptorCyclic plant protein PDP-23 (1 entity in total)
Functional Keywordsmacrocyclic peptide, hydrophobic core, plant protein
Biological sourceZinnia elegans
Total number of polymer chains1
Total formula weight3135.51
Authors
Payne, C.D.,Rosengren, K.J. (deposition date: 2020-12-21, release date: 2021-01-20, Last modification date: 2023-06-14)
Primary citationPayne, 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: 34040741
DOI: 10.1039/d1sc00692d
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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