6D65

Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7

6D65 の概要

• エントリーDOI: 10.2210/pdb6d65/pdb
• 分子名称: Maltose-binding periplasmic protein,Dual specificity protein phosphatase 1, Designed AR protein off7, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: dual specificity phosphatase, dusp, c258s, hydrolase, mbp, darpin
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154553.60

構造登録者

Gumpena, R.,Lountos, G.T.,Waugh, D.S. (登録日: 2018-04-20, 公開日: 2018-09-19, 最終更新日: 2023-10-04)

主引用文献

Gumpena, R.,Lountos, G.T.,Waugh, D.S.
MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.
Acta Crystallogr F Struct Biol Commun, 74:549-557, 2018

PubMed Abstract: The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner, Escherichia coli maltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported.

PubMed: 30198887
DOI: 10.1107/S2053230X18009901

実験手法

X-RAY DIFFRACTION (2.348 Å)