6NU4

Solution structure of the Arabidopsis thaliana RALF8 peptide

Summary for 6NU4

• Entry DOI: 10.2210/pdb6nu4/pdb
• NMR Information: BMRB: 30565
• Descriptor: Protein RALF-like 8 (1 entity in total)
• Functional Keywords: rapid alkalinization factor-8, cysteine-rich plant peptide, plant growth, pollen tube generation, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 6248.08

Authors

Lee, W.,Markley, J.L.,Frederick, R.O.,Miyoshi, H.,Tonelli, M.,Cornilescu, G.,Cornilescu, C.,Sussman, M.R. (deposition date: 2019-01-30, release date: 2019-05-08, Last modification date: 2024-11-06)

Primary citation

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

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: 31004454
DOI: 10.1002/pro.3628

Experimental method

SOLUTION NMR