5EHB
A de novo designed hexameric coiled-coil peptide with iodotyrosine
5EHB の概要
| エントリーDOI | 10.2210/pdb5ehb/pdb |
| 分子名称 | pHiosYI (1 entity in total) |
| 機能のキーワード | coiled-coil, peptide design, 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 | 7706.26 |
| 構造登録者 | Lizatovic, R.,Aurelius, O.,Stenstrom, O.,Drakenberg, T.,Akke, M.,Logan, D.T.,Andre, I. (登録日: 2015-10-28, 公開日: 2016-06-15, 最終更新日: 2024-11-13) |
| 主引用文献 | Lizatovic, R.,Aurelius, O.,Stenstrom, O.,Drakenberg, T.,Akke, M.,Logan, D.T.,Andre, I. A De Novo Designed Coiled-Coil Peptide with a Reversible pH-Induced Oligomerization Switch. Structure, 24:946-955, 2016 Cited by PubMed Abstract: Protein conformational switches have many useful applications but are difficult to design rationally. Here we demonstrate how the isoenergetic energy landscape of higher-order coiled coils can enable the formation of an oligomerization switch by insertion of a single destabilizing element into an otherwise stable computationally designed scaffold. We describe a de novo designed peptide that was discovered to switch between a parallel symmetric pentamer at pH 8 and a trimer of antiparallel dimers at pH 6. The transition between pentamer and hexamer is caused by changes in the protonation states of glutamatic acid residues with highly upshifted pKa values in both oligomer forms. The drastic conformational change coupled with the narrow pH range makes the peptide sequence an attractive candidate for introduction of pH sensing into other proteins. The results highlight the remarkable ability of simple-α helices to self-assemble into a vast range of structural states. PubMed: 27161978DOI: 10.1016/j.str.2016.03.027 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.19 Å) |
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