2DFI

Crystal structure of Pf-MAP(1-292)-C

2DFI の概要

• エントリーDOI: 10.2210/pdb2dfi/pdb
• 関連するPDBエントリー: 1XGM
• 分子名称: Methionine aminopeptidase, COBALT (II) ION (3 entities in total)
• 機能のキーワード: chameleon sequence, fusion protein, methionine aminopeptidase, pyrococcus furiosus, pf-map, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67508.00

構造登録者

Katagiri, Y.,Takano, K.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. (登録日: 2006-03-01, 公開日: 2007-03-06, 最終更新日: 2023-10-25)

主引用文献

Takano, K.,Katagiri, Y.,Mukaiyama, A.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S.
Conformational contagion in a protein: Structural properties of a chameleon sequence
Proteins, 68:617-625, 2007

PubMed Abstract: Certain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases.

PubMed: 17510955
DOI: 10.1002/prot.21451

実験手法

X-RAY DIFFRACTION (2.1 Å)