5O74

Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP

5O74 の概要

• エントリーDOI: 10.2210/pdb5o74/pdb
• 分子名称: Multifunctional virulence effector protein DrrA, Ras-related protein Rab-1B, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: rab1b, drra, exchange factor, legionella pneumophila, hydrolase
• 由来する生物種: Legionella pneumophila; 詳細
• 細胞内の位置: Secreted : Q29ST3; Cytoplasm : Q9H0U4
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 258297.26

構造登録者

Cigler, M.,Mueller, T.,Horn-Ghetko, D.,von Wrisberg, M.K.,Fottner, M.,Goody, R.S.,Itzen, A.,Mueller, M.P.,Lang, K. (登録日: 2017-06-08, 公開日: 2017-10-11, 最終更新日: 2024-01-17)

主引用文献

Cigler, M.,Muller, T.G.,Horn-Ghetko, D.,von Wrisberg, M.K.,Fottner, M.,Goody, R.S.,Itzen, A.,Muller, M.P.,Lang, K.
Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo.
Angew. Chem. Int. Ed. Engl., 56:15737-15741, 2017

PubMed Abstract: The characterization of low-affinity protein complexes is challenging due to their dynamic nature. Here, we present a method to stabilize transient protein complexes in vivo by generating a covalent and conformationally flexible bridge between the interaction partners. A highly active pyrrolysyl tRNA synthetase mutant directs the incorporation of unnatural amino acids bearing bromoalkyl moieties (BrCnK) into proteins. We demonstrate for the first time that low-affinity protein complexes between BrCnK-containing proteins and their binding partners can be stabilized in vivo in bacterial and mammalian cells. Using this approach, we determined the crystal structure of a transient GDP-bound complex between a small G-protein and its nucleotide exchange factor. We envision that this approach will prove valuable as a general tool for validating and characterizing protein-protein interactions in vitro and in vivo.

PubMed: 28960788
DOI: 10.1002/anie.201706927

実験手法

X-RAY DIFFRACTION (2.5 Å)