9IYC
P ring on polyrod-P ring complex from Salmonella TH26292 strain
Summary for 9IYC
| Entry DOI | 10.2210/pdb9iyc/pdb |
| EMDB information | 60995 |
| Descriptor | Flagellar P-ring protein (1 entity in total) |
| Functional Keywords | flagella motor. p ring on polyrod(papr) complex, cryo-em, spa, salmonella, motor protein |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 26 |
| Total formula weight | 943795.32 |
| Authors | Yamaguchi, T.,Kato, T.,Minamino, T.,Namba, K. (deposition date: 2024-07-30, release date: 2026-03-04, Last modification date: 2026-07-29) |
| Primary citation | Yamaguchi, T.,Minamino, T.,Kato, T.,Chevance, F.F.V.,Hughes, K.T.,Namba, K. Structural insights into the assembly mechanism of the molecular bushing in the bacterial flagellar motor. Commun Biol, 2026 Cited by PubMed Abstract: The LP-ring complex of the Salmonella flagellar motor acts as a bushing that supports high-speed rotation of the rod, which serves as a drive shaft. The L-ring, P-ring, and distal rod consist of FlgH, FlgI, and FlgG, respectively. LP-ring formation begins with P-ring assembly around the distal rod, where it remains firmly attached until the L-ring assembles above it. L-ring formation induces P-ring detachment, allowing the rod to freely rotate within the LP-ring, but this mechanism remains unclear. Here, we report the cryoEM structure of the P-ring assembled on a polyrod, an unusually elongated rod structure. The P-ring exhibits a slightly elliptical shape with a 2.7° tilt relative to the rod axis for its stable attachment. However, L-ring assembly on the P-ring causes steric clashes with the rod to induce P-ring detachment, allowing it to adopt a circular shape and complete the LP-ring as a functional bushing. PubMed: 42443432DOI: 10.1038/s42003-026-10640-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.33 Å) |
Structure validation
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