3CKF

The crystal structure of OspA deletion mutant

3CKF の概要

• エントリーDOI: 10.2210/pdb3ckf/pdb
• 関連するPDBエントリー: 3CKA 3CKG
• 分子名称: Outer surface protein A (2 entities in total)
• 機能のキーワード: beta-sheet, membrane protein
• 由来する生物種: Borrelia burgdorferi (Lyme disease spirochete); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23852.65

構造登録者

Makabe, K.,Koide, S. (登録日: 2008-03-14, 公開日: 2009-01-27, 最終更新日: 2023-08-30)

主引用文献

Makabe, K.,Koide, S.
The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion
J.Am.Chem.Soc., 130:14370-14371, 2008

PubMed Abstract: Recent studies suggest the dominant role of main-chain H-bond formation in specifying beta-sheet topology. Its essentially sequence-independent nature implies a large degree of freedom in designing beta-sheet-based nanomaterials. Here we show rational design of beta-sheet face inversions by incremental deletions of beta-strands from the single-layer beta-sheet of Borrelia outer surface protein A. We show that a beta-sheet structure can be maintained when a large number of native contacts are removed and that one can design large-scale conformational transitions of a beta-sheet such as face inversion by exploiting the promiscuity of strand-strand interactions. High-resolution X-ray crystal structures confirmed the success of the design and supported the importance of main-chain H-bonds in determining beta-sheet topology. This work suggests a simple but effective strategy for designing and controlling nanomaterials based on beta-rich peptide self-assemblies.

PubMed: 18842042
DOI: 10.1021/ja805011h

実験手法

X-RAY DIFFRACTION (1.25 Å)