6A42

R1EN(5-223)-ubiquitin fusion

6A42 の概要

• エントリーDOI: 10.2210/pdb6a42/pdb
• 関連するPDBエントリー: 1UBQ 2EI9
• 分子名称: RNA-directed DNA polymerase homolog (R1),Polyubiquitin-C, ACETIC ACID (3 entities in total)
• 機能のキーワード: endonuclease, chimera, dna binding protein
• 由来する生物種: Bombyx mori (Silk moth); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33177.77

構造登録者

Maita, N. (登録日: 2018-06-19, 公開日: 2018-10-24, 最終更新日: 2023-11-22)

主引用文献

Maita, N.
Crystal Structure Determination of Ubiquitin by Fusion to a Protein That Forms a Highly Porous Crystal Lattice
J. Am. Chem. Soc., 140:13546-13549, 2018

PubMed Abstract: The protein crystallization process requires screening of a large number of conditions using a large quantity of high-purity protein, which makes crystal structure analysis difficult. Thus, the development of easy and versatile protein crystallization techniques is both extremely desirable and highly challenging. Here I demonstrate the crystallization and structure determination of ubiquitin by genetic fusion to the highly porous honeycomb lattice of R1EN. I successfully crystallized and collected X-ray data from three R1EN-ubiquitin constructs with various linker lengths under the same conditions as the original R1EN. The crystals diffracted to 1.7-2.4 Å resolution, and the ubiquitin structures were determined with results almost identical to the previously published structure. Moreover, the ubiquitin structure could be solved by molecular replacement using R1EN alone. This method may reduce the effort required for crystallization screening and is applicable to de novo protein structure determination.

PubMed: 30299944
DOI: 10.1021/jacs.8b07512

実験手法

X-RAY DIFFRACTION (1.7 Å)