5INZ

Racemic structure of baboon theta defensin-2

5INZ の概要

• エントリーDOI: 10.2210/pdb5inz/pdb
• 分子名称: Theta defensin-2, L-peptide, Theta defensin-2, D-peptide, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: cyclic peptide, mirror image beta sheet, antibiotic
• 由来する生物種: Papio anubis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 9373.50

構造登録者

Wang, C.K.,King, G.J.,Conibear, A.C.,Ramos, M.C.,Craik, D.J. (登録日: 2016-03-08, 公開日: 2016-04-27, 最終更新日: 2024-10-16)

主引用文献

Wang, C.K.,King, G.J.,Conibear, A.C.,Ramos, M.C.,Chaousis, S.,Henriques, S.T.,Craik, D.J.
Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties.
J.Am.Chem.Soc., 138:5706-5713, 2016

PubMed Abstract: Enantiomeric forms of BTD-2, PG-1, and PM-1 were synthesized to delineate the structure and function of these β-sheet antimicrobial peptides. Activity and lipid-binding assays confirm that these peptides act via a receptor-independent mechanism involving membrane interaction. The racemic crystal structure of BTD-2 solved at 1.45 Å revealed a novel oligomeric form of β-sheet antimicrobial peptides within the unit cell: an antiparallel trimer, which we suggest might be related to its membrane-active form. The BTD-2 oligomer extends into a larger supramolecular state that spans the crystal lattice, featuring a steric-zipper motif that is common in structures of amyloid-forming peptides. The supramolecular structure of BTD-2 thus represents a new mode of fibril-like assembly not previously observed for antimicrobial peptides, providing structural evidence linking antimicrobial and amyloid peptides.

PubMed: 27064294
DOI: 10.1021/jacs.6b02575

実験手法

X-RAY DIFFRACTION (1.447 Å)