9HMF
Periplasmic scaffold of the Campylobacter jejuni flagellar motor (alpha carbon trace)
Summary for 9HMF
| Entry DOI | 10.2210/pdb9hmf/pdb |
| EMDB information | 16724 |
| Descriptor | Flagellar protein FliL, Paralyzed flagella protein PflA, TPR domain protein, ... (6 entities in total) |
| Functional Keywords | molecular machines, flagellar motor, molecular evolution, in situ, scaffold, motor protein, structural protein |
| Biological source | Campylobacter jejuni More |
| Total number of polymer chains | 18 |
| Total formula weight | 665691.23 |
| Authors | Drobnic, T.,Beeby, M. (deposition date: 2024-12-09, release date: 2024-12-25, Last modification date: 2025-07-16) |
| Primary citation | Drobnic, T.,Cohen, E.J.,Calcraft, T.,Alzheimer, M.,Froschauer, K.,Svensson, S.,Hoffman, W.H.,Singh, N.,Garg, S.G.,Henderson, L.D.,Umrekar, T.R.,Nans, A.,Ribardo, D.,Pedaci, F.,Nord, A.L.,Hochberg, G.K.A.,Hendrixson, D.R.,Sharma, C.M.,Rosenthal, P.B.,Beeby, M. In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque. Nat Microbiol, 10:1723-1740, 2025 Cited by PubMed Abstract: The bacterial flagellar motor, which spins a helical propeller for propulsion, has undergone evolutionary diversification across bacterial species, often involving the addition of structures associated with increasing torque for motility in viscous environments. Understanding how such structures function and have evolved is hampered by challenges in visualizing motors in situ. Here we developed a Campylobacter jejuni minicell system for in situ cryogenic electron microscopy imaging and single-particle analysis of its motor, one of the most complex flagellar motors known, to subnanometre resolution. Focusing on the large periplasmic structures which are essential for increasing torque, our structural data, interpreted with molecular models, show that the basal disk comprises concentric rings of FlgP. The medial disk is a lattice of PflC with PflD, while the proximal disk is a rim of PflB attached to spokes of PflA. PflAB dimerization is essential for proximal disk assembly, recruiting FliL to scaffold more stator complexes at a wider radius which increases torque. We also acquired insights into universal principles of flagellar torque generation. This in situ approach is broadly applicable to other membrane-residing bacterial molecular machines. PubMed: 40595286DOI: 10.1038/s41564-025-02012-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.9 Å) |
Structure validation
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