2LA0

Trn- peptide of the two-component bacteriocin Thuricin CD

2LA0 の概要

• エントリーDOI: 10.2210/pdb2la0/pdb
• 関連するPDBエントリー: 2L9X
• NMR情報: BMRB: 17495
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: thioether bridges, helical loops, crosslinked, post-translationally modified, antimicrobial protein
• 由来する生物種: Bacillus cereus 95/8201
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2868.27

構造登録者

Sit, C.S.,Mckay, R.T.,Hill, C.,Ross, R.P.,Vederas, J.C. (登録日: 2011-02-27, 公開日: 2012-01-11, 最終更新日: 2024-10-30)

主引用文献

Sit, C.S.,McKay, R.T.,Hill, C.,Ross, R.P.,Vederas, J.C.
The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links.
J.Am.Chem.Soc., 133:7680-7683, 2011

PubMed Abstract: Thuricin CD is an antimicrobial factor that consists of two peptides, Trn-α and Trn-β, that exhibit synergistic activity against drug resistant strains of Clostridium difficile. Trn-α and Trn-β each possess three sulfur to α-carbon thioether bridges for which the stereochemistry is unknown. This report presents the three-dimensional solution structures of Trn-α and Trn-β. Structure calculations were performed for the eight possible stereoisomers of each peptide based on the same NMR data. The structure of the stereoisomer that best fit the experimental data was chosen as the representative structure for each peptide. It was determined that Trn-α has L-stereochemistry at Ser21 (α-R), L-stereochemistry at Thr25 (α-R), and D-stereochemistry at Thr28 (α-S) (an LLD isomer). Trn-β was also found to be the LLD isomer, with L-stereochemistry at Thr21 (α-R), L-stereochemistry at Ala25 (α-R), and D-stereochemistry at Tyr28 (α-S).

PubMed: 21526839
DOI: 10.1021/ja201802f

実験手法

SOLUTION NMR