6JI7
Coffeetides: iron-binding cysteine rich peptides from coffee waste
Summary for 6JI7
| Entry DOI | 10.2210/pdb6ji7/pdb |
| Descriptor | coffeetide (1 entity in total) |
| Functional Keywords | coffee, cysteine-rich peptide, iron-binding, stable, coffee husk, plant protein |
| Biological source | Coffea canephora |
| Total number of polymer chains | 1 |
| Total formula weight | 3773.33 |
| Authors | Fan, J.S.,Huang, J.Y.,Wong, K.H.,Tay, S.V. (deposition date: 2019-02-20, release date: 2020-02-26, Last modification date: 2025-02-12) |
| Primary citation | Tam, J.P.,Huang, J.,Loo, S.,Li, Y.,Kam, A. Ginsentide-like Coffeetides Isolated from Coffee Waste Are Cell-Penetrating and Metal-Binding Microproteins. Molecules, 28:-, 2023 Cited by PubMed Abstract: Coffee processing generates a huge amount of waste that contains many natural products. Here, we report the discovery of a panel of novel cell-penetrating and metal ion-binding microproteins designated coffeetide cC1a-c and cL1-6 from the husk of two popular coffee plants, and , respectively. Combining sequence determination and a database search, we show that the prototypic coffeetide cC1a is a 37-residue, eight-cysteine microprotein with a hevein-like cysteine motif, but without a chitin-binding domain. NMR determination of cC1a reveals a compact structure that confers its resistance to heat and proteolytic degradation. Disulfide mapping together with chemical synthesis reveals that cC1a has a ginsentide-like, and not a hevein-like, disulfide connectivity. In addition, transcriptomic analysis showed that the 98-residue micrcoproten-like coffeetide precursor contains a three-domain arrangement, like ginsentide precursors. Molecular modeling, together with experimental validation, revealed a Mg and Fe binding pocket at the N-terminus formed by three glutamic acids. Importantly, cC1a is amphipathic with a continuous stretch of 19 apolar amino acids, which enables its cell penetration to target intracellular proteins, despite being highly negatively charged. Our findings suggest that coffee by-products could provide a source of ginsentide-like bioactive peptides that have the potential to target intracellular proteins. PubMed: 37764332DOI: 10.3390/molecules28186556 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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