6I3A

Crystal structure of v22Pizza6-AYW, a circularly permuted designer protein

6I3A の概要

• エントリーDOI: 10.2210/pdb6i3a/pdb
• 分子名称: v22Pizza6-AYW, BROMIDE ION (3 entities in total)
• 機能のキーワード: circularly permuted designer protein, artificial protein, beta-propeller, pizza, 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: 26359.78

構造登録者

Mylemans, B.,Noguchi, H.,Deridder, E.,Voet, A.R.D. (登録日: 2018-11-05, 公開日: 2019-11-20, 最終更新日: 2024-01-24)

主引用文献

Mylemans, B.,Noguchi, H.,Deridder, E.,Lescrinier, E.,Tame, J.R.H.,Voet, A.R.D.
Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.
Protein Sci., 2020

PubMed Abstract: The β-propeller fold is adopted by a sequentially diverse family of repeat proteins with apparent rotational symmetry. While the structure is mostly stabilized by hydrophobic interactions, an additional stabilization is provided by hydrogen bonds between the N-and C-termini, which are almost invariably part of the same β-sheet. This feature is often referred to as the "Velcro" closure. The positioning of the termini within a blade is variable and depends on the protein family. In order to investigate the influence of this location on protein structure, folding and stability, we created different circular permutants, and a circularized version, of the designer propeller protein named Pizza. This protein is perfectly symmetrical, possessing six identical repeats. While all mutants adopt the same structure, the proteins lacking the "Velcro" closure were found to be significantly less resistant to thermal and chemical denaturation. This could explain why such proteins are rarely observed in nature. Interestingly the most common "Velcro" configuration for this protein family was not the most stable among the Pizza variants tested. The circularized version shows dramatically improved stability, which could have implications for future applications.

PubMed: 33006397
DOI: 10.1002/pro.3961

実験手法

X-RAY DIFFRACTION (1.45 Å)