7CKD
Solution structure of NCR169 oxidized form 1 from Medicago truncatula
Summary for 7CKD
| Entry DOI | 10.2210/pdb7ckd/pdb |
| NMR Information | BMRB: 36362 |
| Descriptor | Nodule Cysteine-Rich (NCR) secreted peptide (1 entity in total) |
| Functional Keywords | medicago truncatula, nodule-specific cysteine-rich peptide, antimicrobial peptide, disulfide bond, plant protein |
| Biological source | Medicago truncatula (Barrel medic) |
| Total number of polymer chains | 1 |
| Total formula weight | 4630.52 |
| Authors | Isozumi, N.,Masubuchi, Y.,Ohki, S. (deposition date: 2020-07-16, release date: 2021-05-26, Last modification date: 2024-10-30) |
| Primary citation | Isozumi, N.,Masubuchi, Y.,Imamura, T.,Mori, M.,Koga, H.,Ohki, S. Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. Sci Rep, 11:9923-9923, 2021 Cited by PubMed Abstract: A model legume, Medicago truncatula, has over 600 nodule-specific cysteine-rich (NCR) peptides required for symbiosis with rhizobia. Among them, NCR169, an essential factor for establishing symbiosis, has four cysteine residues that are indispensable for its function. However, knowledge of NCR169 structure and mechanism of action is still lacking. In this study, we solved two NMR structures of NCR169 caused by different disulfide linkage patterns. We show that both structures have a consensus C-terminal β-sheet attached to an extended N-terminal region with dissimilar features; one moves widely, whereas the other is relatively stapled. We further revealed that the disulfide bonds of NCR169 contribute to its structural stability and solubility. Regarding the function, one of the NCR169 oxidized forms could bind to negatively charged bacterial phospholipids. Furthermore, the positively charged lysine-rich region of NCR169 may be responsible for its antimicrobial activity against Escherichia coli and Sinorhizobium meliloti. This active region was disordered even in the phospholipid bound state, suggesting that the disordered conformation of this region is key to its function. Morphological observations suggested the mechanism of action of NCR169 on bacteria. The present study on NCR169 provides new insights into the structure and function of NCR peptides. PubMed: 33972675DOI: 10.1038/s41598-021-89485-w PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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