5IQO

Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitutions Q134E and S138E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_T4R-T6R-D13N

5IQO の概要

• エントリーDOI: 10.2210/pdb5iqo/pdb
• 分子名称: Protein FimG, Protein FimF, COBALT (II) ION, ... (6 entities in total)
• 機能のキーワード: complex, protein, fimgt, cell adhesion
• 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: 31514.65

構造登録者

Giese, C.,Eras, J.,Kern, A.,Capitani, G.,Glockshuber, R. (登録日: 2016-03-11, 公開日: 2016-07-06, 最終更新日: 2024-10-09)

主引用文献

Giese, C.,Eras, J.,Kern, A.,Scharer, M.A.,Capitani, G.,Glockshuber, R.
Accelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of Magnitude.
Angew.Chem.Int.Ed.Engl., 55:9350-9355, 2016

PubMed Abstract: The complex between the bacterial type 1 pilus subunit FimG and the peptide corresponding to the N-terminal extension (termed donor strand, Ds) of the partner subunit FimF (DsF) shows the strongest reported noncovalent molecular interaction, with a dissociation constant (KD ) of 1.5×10(-20)  m. However, the complex only exhibits a slow association rate of 330 m(-1)  s(-1) that limits technical applications, such as its use in affinity purification. Herein, a structure-based approach was used to design pairs of FimGt (a FimG variant lacking its own N-terminal extension) and DsF variants with enhanced electrostatic surface complementarity. Association of the best mutant FimGt/DsF pairs was accelerated by more than two orders of magnitude, while the dissociation rates and 3D structures of the improved complexes remained essentially unperturbed. A KD  value of 8.8×10(-22)  m was obtained for the best mutant complex, which is the lowest value reported to date for a protein/ligand complex.

PubMed: 27351462
DOI: 10.1002/anie.201603652

実験手法

X-RAY DIFFRACTION (1.302 Å)