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CryoEM structure of the type IV pilin PilA4 from Thermus thermophilus
Structural highlights
FunctionPILA4_THET2 Plays an essential role in the assembly of two types of T4P pili: a wide and a narrow that participate in natural transformation and twitching motility (PubMed:32376942). Major component of the wide pilus that is essential for natural transformation working as a DNA translocator structure that spans the inner and outer membranes (PubMed:12839734, PubMed:16857013, PubMed:19396940, PubMed:32376942). In addition, participates in the assembly of the narrow pilus composed of the PilA5 subunit that is required for twitching motility (PubMed:32376942).[1] [2] [3] [4] Publication Abstract from PubMedType 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. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.,Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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