7CKD

Solution structure of NCR169 oxidized form 1 from Medicago truncatula

7CKD の概要

• エントリーDOI: 10.2210/pdb7ckd/pdb
• 分子名称: Nodule Cysteine-Rich (NCR) secreted peptide (1 entity in total)
• 機能のキーワード: medicago truncatula, nodule-specific cysteine-rich peptide, antimicrobial peptide, disulfide bond, plant protein
• 由来する生物種: Medicago truncatula (Barrel medic)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4630.52

構造登録者

Isozumi, N.,Masubuchi, Y.,Ohki, S. (登録日: 2020-07-16, 公開日: 2021-05-26, 最終更新日: 2024-10-30)

主引用文献

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

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: 33972675
DOI: 10.1038/s41598-021-89485-w

実験手法

SOLUTION NMR