6QEV

EngBF DARPin Fusion 4b B6

6QEV の概要

• エントリーDOI: 10.2210/pdb6qev/pdb
• 関連するPDBエントリー: 6QEP
• 分子名称: PEGA domain-containing protein,PEGA domain-containing protein,EngBF DARPin fusion B6 complex, PRO-LYS-SER-ILE-ARG-ILE-GLY-PRO-GLY-GLN-ALA-PHE-TYR-ALA-DPR, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: crystallization chaperone, protein fusion, darpin, chaperone, hydrolase
• 由来する生物種: Bifidobacterium longum; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 150023.73

構造登録者

Ernst, P.,Pluckthun, A.,Mittl, P.R.E. (登録日: 2019-01-08, 公開日: 2019-11-06, 最終更新日: 2024-10-23)

主引用文献

Ernst, P.,Pluckthun, A.,Mittl, P.R.E.
Structural analysis of biological targets by host:guest crystal lattice engineering.
Sci Rep, 9:15199-15199, 2019

PubMed Abstract: To overcome the laborious identification of crystallisation conditions for protein X-ray crystallography, we developed a method where the examined protein is immobilised as a guest molecule in a universal host lattice. We applied crystal engineering to create a generic crystalline host lattice under reproducible, predefined conditions and analysed the structures of target guest molecules of different size, namely two 15-mer peptides and green fluorescent protein (sfGFP). A fusion protein with an N-terminal endo-α-N-acetylgalactosaminidase (EngBF) domain and a C-terminal designed ankyrin repeat protein (DARPin) domain establishes the crystal lattice. The target is recruited into the host lattice, always in the same crystal form, through binding to the DARPin. The target structures can be determined rapidly from difference Fourier maps, whose quality depends on the size of the target and the orientation of the DARPin.

PubMed: 31645583
DOI: 10.1038/s41598-019-51017-y

実験手法

X-RAY DIFFRACTION (2.7 Å)