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-Structure paper
タイトル | The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 3032, Year 2024 |
掲載日 | 2024年4月8日 |
著者 | Dawid S Zyla / Thomas Wiegand / Paul Bachmann / Rafal Zdanowicz / Christoph Giese / Beat H Meier / Gabriel Waksman / Manuela K Hospenthal / Rudi Glockshuber / |
PubMed 要旨 | Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of ...Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure. |
リンク | Nat Commun / PubMed:38589417 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.52 - 2.85 Å |
構造データ | EMDB-10721, PDB-6y7s: EMDB-17863, PDB-8psv: EMDB-17878, PDB-8ptu: |
由来 |
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キーワード | STRUCTURAL PROTEIN / FimA / pilus / monomer / subunit / pili / main structural subunit / high resolution / cryo-EM / helical processing / RELION / Chaperone-usher pilus |