6F0T

Crystal structure of Pizza6-SFW

6F0T の概要

• エントリーDOI: 10.2210/pdb6f0t/pdb
• 分子名称: Pizza6-SFW, GLYCEROL (3 entities in total)
• 機能のキーワード: artificial protein, beta propeller, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77693.39

構造登録者

Noguchi, H.,De Zitter, E.,Van Meervelt, L.,Voet, A.R.D. (登録日: 2017-11-20, 公開日: 2018-03-21, 最終更新日: 2024-05-08)

主引用文献

Noguchi, H.,Mylemans, B.,De Zitter, E.,Van Meervelt, L.,Tame, J.R.H.,Voet, A.
Design of tryptophan-containing mutants of the symmetrical Pizza protein for biophysical studies.
Biochem. Biophys. Res. Commun., 497:1038-1042, 2018

PubMed Abstract: β-propeller proteins are highly symmetrical, being composed of a repeated motif with four anti-parallel β-sheets arranged around a central axis. Recently we designed the first completely symmetrical β-propeller protein, Pizza6, consisting of six identical tandem repeats. Pizza6 is expected to prove a useful building block for bionanotechnology, and also a tool to investigate the folding and evolution of β-propeller proteins. Folding studies are made difficult by the high stability and the lack of buried Trp residues to act as monitor fluorophores, so we have designed and characterized several Trp-containing Pizza6 derivatives. In total four proteins were designed, of which three could be purified and characterized. Crystal structures confirm these mutant proteins maintain the expected structure, and a clear redshift of Trp fluorescence emission could be observed upon denaturation. Among the derivative proteins, Pizza6-AYW appears to be the most suitable model protein for future folding/unfolding kinetics studies as it has a comparable stability as natural β-propeller proteins.

PubMed: 29481797
DOI: 10.1016/j.bbrc.2018.02.168

実験手法

X-RAY DIFFRACTION (1.74 Å)