NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana
Copyright © 2016 Elsevier B.V. All rights reserved..
Plant defensins constitute the innate immune response against pathogens such as fungi and bacteria. Typical plant defensins are small, basic peptides that possess a characteristic three-dimensional fold stabilized by three or four disulfide bridges. In addition to known defensin genes, the Arabidopsis genome comprises >300 defensin-like genes coding for small cysteine-rich peptides. One of such genes encodes for AtPDFL2.1, a putative antifungal peptide of 55 amino acids, with six cysteine residues in its primary sequence. To understand the functional role of AtPDFL2.1, we carried out antifungal activity assays and determined its high-resolution three-dimensional structure using multidimensional solution NMR spectroscopy. We found that AtPDFL2.1 displays a strong inhibitory effect against Fusarium graminearum (IC50≈4μM). This peptide folds in the canonical cysteine-stabilized αβ (CSαβ) motif, consisting of one α-helix and one triple-stranded antiparallel β-sheet stabilized by three disulfide bridges and a hydrophobic cluster of residues within its core where the α-helix packs tightly against the β-sheets. Nuclear spin relaxation measurements show that the structure of AtPDFL2.1 is essentially rigid, with the L3 loop located between β-strands 2 and 3 being more flexible and displaying conformational exchange. Interestingly, the dynamic features of loop L3 are conserved among defensins and are probably correlated to the antifungal and receptor binding activities.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2016 |
|---|---|
| Erschienen: |
2016 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:1864 |
|---|---|
| Enthalten in: |
Biochimica et biophysica acta - 1864(2016), 12 vom: 29. Dez., Seite 1739-1747 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Omidvar, Reza [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 28.01.2019 Date Revised 28.01.2019 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1016/j.bbapap.2016.08.017 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM264030737 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM264030737 | ||
| 003 | DE-627 | ||
| 005 | 20231224205211.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231224s2016 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.bbapap.2016.08.017 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0880.xml |
| 035 | |a (DE-627)NLM264030737 | ||
| 035 | |a (NLM)27592418 | ||
| 035 | |a (PII)S1570-9639(16)30179-0 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Omidvar, Reza |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana |
| 264 | 1 | |c 2016 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 28.01.2019 | ||
| 500 | |a Date Revised 28.01.2019 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2016 Elsevier B.V. All rights reserved. | ||
| 520 | |a Plant defensins constitute the innate immune response against pathogens such as fungi and bacteria. Typical plant defensins are small, basic peptides that possess a characteristic three-dimensional fold stabilized by three or four disulfide bridges. In addition to known defensin genes, the Arabidopsis genome comprises >300 defensin-like genes coding for small cysteine-rich peptides. One of such genes encodes for AtPDFL2.1, a putative antifungal peptide of 55 amino acids, with six cysteine residues in its primary sequence. To understand the functional role of AtPDFL2.1, we carried out antifungal activity assays and determined its high-resolution three-dimensional structure using multidimensional solution NMR spectroscopy. We found that AtPDFL2.1 displays a strong inhibitory effect against Fusarium graminearum (IC50≈4μM). This peptide folds in the canonical cysteine-stabilized αβ (CSαβ) motif, consisting of one α-helix and one triple-stranded antiparallel β-sheet stabilized by three disulfide bridges and a hydrophobic cluster of residues within its core where the α-helix packs tightly against the β-sheets. Nuclear spin relaxation measurements show that the structure of AtPDFL2.1 is essentially rigid, with the L3 loop located between β-strands 2 and 3 being more flexible and displaying conformational exchange. Interestingly, the dynamic features of loop L3 are conserved among defensins and are probably correlated to the antifungal and receptor binding activities | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Antifungal activity | |
| 650 | 4 | |a AtPDFL2.1 | |
| 650 | 4 | |a Conformational dynamics | |
| 650 | 4 | |a Plant defensins | |
| 650 | 4 | |a Solution NMR | |
| 650 | 4 | |a Three-dimensional structure | |
| 650 | 7 | |a Antifungal Agents |2 NLM | |
| 650 | 7 | |a Arabidopsis Proteins |2 NLM | |
| 650 | 7 | |a Defensins |2 NLM | |
| 700 | 1 | |a Xia, Youlin |e verfasserin |4 aut | |
| 700 | 1 | |a Porcelli, Fernando |e verfasserin |4 aut | |
| 700 | 1 | |a Bohlmann, Holger |e verfasserin |4 aut | |
| 700 | 1 | |a Veglia, Gianluigi |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochimica et biophysica acta |d 1948 |g 1864(2016), 12 vom: 29. Dez., Seite 1739-1747 |w (DE-627)NLM000000698 |x 0006-3002 |7 nnns |
| 773 | 1 | 8 | |g volume:1864 |g year:2016 |g number:12 |g day:29 |g month:12 |g pages:1739-1747 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.bbapap.2016.08.017 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 1864 |j 2016 |e 12 |b 29 |c 12 |h 1739-1747 | ||