9BNH

X-ray Crystal Structure of Cu-TZ4H tryptophan Zipper Metallo-Peptide

9BNH の概要

• エントリーDOI: 10.2210/pdb9bnh/pdb
• 分子名称: Cu-TZ4H tryptophan Zipper Metallo-Peptide, AMMONIA, ACETIC ACID, ... (7 entities in total)
• 機能のキーワード: copper, beta-sheet, hairpin, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 4183.38

構造登録者

Dang, V.T.,Nguyen, A. (登録日: 2024-05-02, 公開日: 2024-09-04, 最終更新日: 2024-11-06)

主引用文献

Thuc Dang, V.,Engineer, A.,McElheny, D.,Drena, A.,Telser, J.,Tomczak, K.,Nguyen, A.I.
Crystallography Reveals Metal-Triggered Restructuring of beta-Hairpins.
Chemistry, 30:e202402101-e202402101, 2024

PubMed Abstract: Metal binding to β-sheets occurs in many metalloproteins and is also implicated in the pathology of Alzheimer's disease. De novo designed metallo-β-sheets have been pursued as models and mimics of these proteins. However, no crystal structures of canonical β-sheet metallopeptides have yet been obtained, in stark contrast to many examples for ɑ-helical metallopeptides, leading to a poor understanding for their chemistry. To address this, we have engineered tryptophan zippers, stable 12-residue β-sheet peptides, to bind Cu(II) ions and obtained crystal structures through single crystal X-ray diffraction (SC-XRD). We find that metal binding triggers several unexpected supramolecular assemblies that demonstrate the range of higher-order structures available to metallo-β-sheets. Overall, these findings underscore the importance of crystallography in elucidating the rich structural landscape of metallo-β-sheet peptides.

PubMed: 39152095
DOI: 10.1002/chem.202402101

実験手法

X-RAY DIFFRACTION (1.12 Å)