6NU4
Solution structure of the Arabidopsis thaliana RALF8 peptide
6NU4 の概要
| エントリーDOI | 10.2210/pdb6nu4/pdb |
| NMR情報 | BMRB: 30565 |
| 分子名称 | Protein RALF-like 8 (1 entity in total) |
| 機能のキーワード | rapid alkalinization factor-8, cysteine-rich plant peptide, plant growth, pollen tube generation, plant protein |
| 由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6248.08 |
| 構造登録者 | Lee, W.,Markley, J.L.,Frederick, R.O.,Miyoshi, H.,Tonelli, M.,Cornilescu, G.,Cornilescu, C.,Sussman, M.R. (登録日: 2019-01-30, 公開日: 2019-05-08, 最終更新日: 2024-11-06) |
| 主引用文献 | Frederick, R.O.,Haruta, M.,Tonelli, M.,Lee, W.,Cornilescu, G.,Cornilescu, C.C.,Sussman, M.R.,Markley, J.L. Function and solution structure of the Arabidopsis thaliana RALF8 peptide. Protein Sci., 28:1115-1126, 2019 Cited by PubMed Abstract: We report the recombinant preparation from Escherichia coli cells of samples of two closely related, small, secreted cysteine-rich plant peptides: rapid alkalinization factor 1 (RALF1) and rapid alkalinization factor 8 (RALF8). Purified samples of the native sequence of RALF8 exhibited well-resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression. By contrast, RALF1 could only be isolated from inclusion bodies as a construct containing an N-terminal His-tag; its poorly resolved NMR spectrum was indicative of aggregation. We prepared samples of the RALF8 peptide labeled with N and C for NMR analysis and obtained near complete H, C, and N NMR assignments; determined the disulfide pairing of its four cysteine residues; and examined its solution structure. RALF8 is mostly disordered except for the two loops spanned by each of its two disulfide bridges. PubMed: 31004454DOI: 10.1002/pro.3628 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
構造検証レポート
検証レポート(詳細版)
をダウンロード






