3OGF

Crystal structure of Difoil-4P homo-trimer: de novo designed dimeric trefoil-fold sub-domain which forms homo-trimer assembly

3OGF の概要

• エントリーDOI: 10.2210/pdb3ogf/pdb
• 関連するPDBエントリー: 1JQZ
• 分子名称: de novo designed dimeric trefoil-fold sub-domain which forms homo-trimer assembly, SULFATE ION (2 entities in total)
• 機能のキーワード: beta-trefoil, de novo protein
• 由来する生物種: synthetic construct (artificial gene)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30506.88

構造登録者

Lee, J.,Blaber, M. (登録日: 2010-08-16, 公開日: 2010-12-22, 最終更新日: 2024-02-21)

主引用文献

Lee, J.,Blaber, M.
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Proc.Natl.Acad.Sci.USA, 108:126-130, 2011

PubMed Abstract: The majority of protein architectures exhibit elements of structural symmetry, and "gene duplication and fusion" is the evolutionary mechanism generally hypothesized to be responsible for their emergence from simple peptide motifs. Despite the central importance of the gene duplication and fusion hypothesis, experimental support for a plausible evolutionary pathway for a specific protein architecture has yet to be effectively demonstrated. To address this question, a unique "top-down symmetric deconstruction" strategy was utilized to successfully identify a simple peptide motif capable of recapitulating, via gene duplication and fusion processes, a symmetric protein architecture (the threefold symmetric β-trefoil fold). The folding properties of intermediary forms in this deconstruction agree precisely with a previously proposed "conserved architecture" model for symmetric protein evolution. Furthermore, a route through foldable sequence-space between the simple peptide motif and extant protein fold is demonstrated. These results provide compelling experimental support for a plausible evolutionary pathway of symmetric protein architecture via gene duplication and fusion processes.

PubMed: 21173271
DOI: 10.1073/pnas.1015032108

実験手法

X-RAY DIFFRACTION (2.864 Å)