Structural highlights
Function
FIMG_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
Publication Abstract from PubMed
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 1.5x10-20 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 8.8x10-22 m was obtained for the best mutant complex, which is the lowest value reported to date for a protein/ligand complex.
Accelerating the Association of the Most Stable Protein-Ligand Complex by more than Two Orders of Magnitude.,Giese C, Eras J, Kern A, Scharer MA, Capitani G, Glockshuber R Angew Chem Int Ed Engl. 2016 Jun 28. doi: 10.1002/anie.201603652. PMID:27351462[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Giese C, Eras J, Kern A, Scharer MA, 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. 2016 Jun 28. doi: 10.1002/anie.201603652. PMID:27351462 doi:http://dx.doi.org/10.1002/anie.201603652
