5CWD

Crystal structure of de novo designed helical repeat protein DHR7

5CWD の概要

• エントリーDOI: 10.2210/pdb5cwd/pdb
• 関連するPDBエントリー: 5CWB 5CWC 5CWF 5CWG 5CWH 5CWI 5CWJ 5CWK 5CWL 5CWM 5CWN 5CWO 5CWP 5CWQ
• 分子名称: Designed helical repeat protein (1 entity in total)
• 機能のキーワード: helical repeat protein, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19102.57

構造登録者

Bhabha, G.,Ekiert, D.C. (登録日: 2015-07-28, 公開日: 2015-12-16, 最終更新日: 2024-10-09)

主引用文献

Brunette, T.J.,Parmeggiani, F.,Huang, P.S.,Bhabha, G.,Ekiert, D.C.,Tsutakawa, S.E.,Hura, G.L.,Tainer, J.A.,Baker, D.
Exploring the repeat protein universe through computational protein design.
Nature, 528:580-584, 2015

PubMed Abstract: A central question in protein evolution is the extent to which naturally occurring proteins sample the space of folded structures accessible to the polypeptide chain. Repeat proteins composed of multiple tandem copies of a modular structure unit are widespread in nature and have critical roles in molecular recognition, signalling, and other essential biological processes. Naturally occurring repeat proteins have been re-engineered for molecular recognition and modular scaffolding applications. Here we use computational protein design to investigate the space of folded structures that can be generated by tandem repeating a simple helix-loop-helix-loop structural motif. Eighty-three designs with sequences unrelated to known repeat proteins were experimentally characterized. Of these, 53 are monomeric and stable at 95 °C, and 43 have solution X-ray scattering spectra consistent with the design models. Crystal structures of 15 designs spanning a broad range of curvatures are in close agreement with the design models with root mean square deviations ranging from 0.7 to 2.5 Å. Our results show that existing repeat proteins occupy only a small fraction of the possible repeat protein sequence and structure space and that it is possible to design novel repeat proteins with precisely specified geometries, opening up a wide array of new possibilities for biomolecular engineering.

PubMed: 26675729
DOI: 10.1038/nature16162

実験手法

X-RAY DIFFRACTION (2.61 Å)