7BW5

a new lasso peptide koreensin

7BW5 の概要

• エントリーDOI: 10.2210/pdb7bw5/pdb
• NMR情報: BMRB: 36343
• 分子名称: lasso peptide koreensin (1 entity in total)
• 機能のキーワード: lasso peptide, unknown function
• 由来する生物種: Sphingomonas koreensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1672.84

構造登録者

Hemmi, H.,Kodani, S. (登録日: 2020-04-13, 公開日: 2020-09-09, 最終更新日: 2024-05-15)

主引用文献

Fuwa, H.,Hemmi, H.,Kaweewan, I.,Kozaki, I.,Honda, H.,Kodani, S.
Heterologous production of new lasso peptide koreensin based on genome mining.
J Antibiot (Tokyo), 74:42-50, 2021

PubMed Abstract: Lasso peptides are a class of ribosomally biosynthesized and posttranslationally modified peptides with a knot structure as a common motif. Based on a genome search, a new biosynthetic gene cluster of lasso peptide was found in the genome of the proteobacterium Sphingomonas koreensis. Interestingly, the amino acid sequence of the precursor peptide gene includes two cell adhesion motif sequences (KGD and DGR). Heterologous production of the new lasso peptide was performed using the cryptic biosynthetic gene cluster of S. koreensis. As a result, a new lasso peptide named koreensin was produced by the gene expression system in the host strain Sphingomonas subterranea. The structure of koreensin was determined by NMR and ESI-MS analysis. The three-dimensional structure of koreensin was obtained based on an NOE experiment and the coupling constants. A variant peptide (koreensin-RGD), which had RGD instead of KGD, was produced by heterologous production with site-directed mutagenesis experiment. Koreensin and koreensin-RGD did not show cell adhesion inhibitory activity, although the molecules possessed cell adhesion motifs. The possible presence of a salt bridge between the motifs in koreensin was indicated, and it may prevent the cell adhesion motif from functioning.

PubMed: 32855516
DOI: 10.1038/s41429-020-00363-5

実験手法

SOLUTION NMR