6XXD
CryoEM structure of the type IV pilin PilA4 from Thermus thermophilus
Summary for 6XXD
| Entry DOI | 10.2210/pdb6xxd/pdb |
| EMDB information | 10647 |
| Descriptor | PilA (1 entity in total) |
| Functional Keywords | type iv pilin glycosylation twitching motility, cell adhesion |
| Biological source | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) |
| Total number of polymer chains | 16 |
| Total formula weight | 212017.97 |
| Authors | Neuhaus, A.,Gold, V.A.M. (deposition date: 2020-01-27, release date: 2020-03-11, Last modification date: 2024-11-20) |
| Primary citation | Neuhaus, A.,Selvaraj, M.,Salzer, R.,Langer, J.D.,Kruse, K.,Kirchner, L.,Sanders, K.,Daum, B.,Averhoff, B.,Gold, V.A.M. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun, 11:2231-2231, 2020 Cited by 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 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. PubMed: 32376942DOI: 10.1038/s41467-020-15650-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.22 Å) |
Structure validation
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