6Q8D

Structure of Fucosylated D-antimicrobial peptide SB15 in complex with the Fucose-binding lectin PA-IIL at 1.630 Angstrom resolution

6Q8D の概要

• エントリーDOI: 10.2210/pdb6q8d/pdb
• 関連するPDBエントリー: 6Q6W 6Q6X 6Q77 6Q79 6Q85 6Q86 6Q87
• 分子名称: Fucose-binding lectin, SB15, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: antimicrobial, lectin, complex, antibiotic
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13324.74

構造登録者

Baeriswyl, S.,Stocker, A.,Reymond, J.-L. (登録日: 2018-12-14, 公開日: 2019-03-20, 最終更新日: 2024-11-06)

主引用文献

Baeriswyl, S.,Gan, B.H.,Siriwardena, T.N.,Visini, R.,Robadey, M.,Javor, S.,Stocker, A.,Darbre, T.,Reymond, J.L.
X-ray Crystal Structures of Short Antimicrobial Peptides as Pseudomonas aeruginosa Lectin B Complexes.
Acs Chem.Biol., 14:758-766, 2019

PubMed Abstract: Herein, we report X-ray crystal structures of 11-13 residue antimicrobial peptides (AMPs) active against Pseudomonas aeruginosa as complexes of fucosylated d-enantiomeric sequences with the P. aeruginosa lectin LecB. These represent the first crystal structures of short AMPs. In 24 individual structures of eight different peptides, we found mostly α-helices assembled as two-helix or four-helix bundles with a hydrophobic core and cationic residues pointing outside. Two of the analogs formed an extended structure engaging in multiple contacts with the lectin. Molecular dynamics (MD) simulations showed that α-helices are stabilized by bundle formation and suggested that the N-terminal acyl group present in the linker to the fucosyl group can extend the helix by one additional H-bond and increase α-helix amphiphilicity. Investigating N-terminal acylation led to AMPs with equivalent and partly stronger antibacterial effects compared to the free peptide.

PubMed: 30830745
DOI: 10.1021/acschembio.9b00047

実験手法

X-RAY DIFFRACTION (1.63 Å)