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Molecular Biophysics
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- Protein Structure and FoldingOpen Access
Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria
Journal of Biological ChemistryVol. 294Issue 27p10553–10563Published online: May 24, 2019- Dawid S. Żyła
- Andrea E. Prota
- Guido Capitani
- Rudi Glockshuber
Cited in Scopus: 3Adhesive type 1 pili from enteroinvasive, Gram-negative bacteria mediate attachment to host cells. Up to 3000 copies of the main pilus subunit, FimA, assemble into the filamentous, helical quaternary structure of the pilus rod via a mechanism termed donor-strand complementation, in which the N-terminal extension of each subunit, the donor strand, is inserted into the incomplete immunoglobulin-like fold of the preceding FimA subunit. For FimA from Escherichia coli, it has been previously shown that the protein can also adopt a monomeric, self-complemented conformation in which the donor strand is inserted intramolecularly in the opposite orientation relative to that observed for FimA polymers.