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-Structure paper
Title | Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. |
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Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 2231, Year 2020 |
Publish date | May 6, 2020 |
Authors | Alexander Neuhaus / Muniyandi Selvaraj / Ralf Salzer / Julian D Langer / Kerstin Kruse / Lennart Kirchner / Kelly Sanders / Bertram Daum / Beate Averhoff / Vicki A M Gold / |
PubMed Abstract | Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm ...Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility. |
External links | Nat Commun / PubMed:32376942 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.22 - 3.49 Å |
Structure data | EMDB-10647: CryoEM structure of the wide type IV pilus (PilA4) from Thermus thermophilus EMDB-10648: CryoEM structure of the narrow type IV pilus (PilA5) from Thermus thermophilus |
Source |
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Keywords | CELL ADHESION / Type IV pilin glycosylation twitching motility |