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Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a co...

Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a co...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2528219308

Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core

About this item

Full title

Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core

Publisher

United States: Public Library of Science

Journal title

PLoS pathogens, 2021-04, Vol.17 (4), p.e1009440-e1009440

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

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-affinity state (HAS) conformation allosterically upon mannose bindi...

Alternative Titles

Full title

Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_2528219308

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2528219308

Other Identifiers

ISSN

1553-7374,1553-7366

E-ISSN

1553-7374

DOI

10.1371/journal.ppat.1009440

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