1WN8

NMR Structure of OaNTR

1WN8 の概要

• エントリーDOI: 10.2210/pdb1wn8/pdb
• 関連するPDBエントリー: 1WN4
• 分子名称: Kalata B3/B6 (1 entity in total)
• 機能のキーワード: helix, plant protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2441.92

構造登録者

Dutton, J.L.,Renda, R.F.,Waine, C.,Clark, R.J.,Daly, N.L.,Jennings, C.V.,Anderson, M.A.,Craik, D.J. (登録日: 2004-07-28, 公開日: 2004-09-14, 最終更新日: 2024-05-29)

主引用文献

Dutton, J.L.,Renda, R.F.,Waine, C.,Clark, R.J.,Daly, N.L.,Jennings, C.V.,Anderson, M.A.,Craik, D.J.
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins
J.Biol.Chem., 279:46858-46867, 2004

PubMed Abstract: The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis. Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved alpha-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.

PubMed: 15328347
DOI: 10.1074/jbc.M407421200

実験手法

SOLUTION NMR