Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core.
Critical molecular events that control conformational transitions in most allosteric proteins are ill-defined. The mannose-specific FimH protein of Escherichia coli is a prototypic bacterial adhesin that switches from an 'inactive' low-affinity state (LAS) to an 'active' high-aff...
Main Authors: | Dagmara I Kisiela, Pearl Magala, Gianluca Interlandi, Laura A Carlucci, Angelo Ramos, Veronika Tchesnokova, Benjamin Basanta, Vladimir Yarov-Yarovoy, Hovhannes Avagyan, Anahit Hovhannisyan, Wendy E Thomas, Ronald E Stenkamp, Rachel E Klevit, Evgeni V Sokurenko |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2021-04-01
|
Series: | PLoS Pathogens |
Online Access: | https://doi.org/10.1371/journal.ppat.1009440 |
Similar Items
-
Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coli.
by: Dagmara I Kisiela, et al.
Published: (2015-05-01) -
Evolution of Salmonella enterica virulence via point mutations in the fimbrial adhesin.
by: Dagmara I Kisiela, et al.
Published: (2012-01-01) -
Repacking on Demand for Hierarchical Cellular Networks
by: Yung-Chun Lin, et al.
Published: (2003) -
Storage duration effect on deformation recovery of repacked alginates
by: Siti Sunarintyas, et al.
Published: (2009-09-01) -
Point mutations in FimH adhesin of Crohn's disease-associated adherent-invasive Escherichia coli enhance intestinal inflammatory response.
by: Nicolas Dreux, et al.
Published: (2013-01-01)