9IUG
Cryo-EM structure of the type I pilus from enterotoxigenic Escherichia coli
Summary for 9IUG
| Entry DOI | 10.2210/pdb9iug/pdb |
| EMDB information | 60903 |
| Descriptor | FimA (2 entities in total) |
| Functional Keywords | type 1 pili, fima, cell adhesion |
| Biological source | Escherichia coli |
| Total number of polymer chains | 21 |
| Total formula weight | 343643.83 |
| Authors | Kawahara, K.,Oki, H.,Nakamura, S. (deposition date: 2024-07-21, release date: 2025-05-28, Last modification date: 2025-06-25) |
| Primary citation | Kawahara, K.,Oki, H.,Iimori, M.,Muramoto, R.,Imai, T.,Gerle, C.,Shigematsu, H.,Matsuda, S.,Iida, T.,Nakamura, S. High-resolution cryo-EM analysis visualizes hydrated type I and IV pilus structures from enterotoxigenic Escherichia coli. Structure, 33:1040-, 2025 Cited by PubMed Abstract: Pathogenic bacteria utilize a variety of pilus filaments to colonize intestinal epithelia, including those synthesized by the chaperone-usher or type IV pilus assembly pathway. Despite the importance of these filaments as potential drug and vaccine targets, their large size and dynamic nature make high-resolution structure determination challenging. Here, we used cryo-electron microscopy (cryo-EM) and whole-genome sequencing to determine the structures of type I and IV pili expressed in enterotoxigenic Escherichia coli. Well-defined cryo-EM maps at resolutions of 2.2 and 1.8 Å for type I and IV pilus, respectively, facilitated the de novo structural modeling for these filaments, revealing side-chain structures in detail. We resolved thousands of hydrated water molecules around and within the inner core of the filaments, which stabilize the otherwise metastable quaternary subunit assembly. The high-resolution structures offer novel insights into subunit-subunit interactions, and provide important clues to understand pilus assembly, stability, and flexibility. PubMed: 40220752DOI: 10.1016/j.str.2025.03.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.2 Å) |
Structure validation
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