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 | |
| Primary citation | Drobnic, T.,Cohen, E.J.,Calcraft, T.,Alzheimer, M.,Froschauer, K.,Svensson, S.,Hoffmann, W.H.,Singh, N.,Garg, S.G.,Henderson, L.,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. Molecular model of a bacterial flagellar motor in situ reveals a "parts-list" of protein adaptations to increase torque. Biorxiv, 2024 Cited by PubMed Abstract: One hurdle to understanding how molecular machines work, and how they evolve, is our inability to see their structures . Here we describe a minicell system that enables cryogenic electron microscopy imaging and single particle analysis to investigate the structure of an iconic molecular machine, the bacterial flagellar motor, which spins a helical propeller for propulsion. We determine the structure of the high-torque motor including the subnanometre-resolution structure of the periplasmic scaffold, an adaptation essential to high torque. Our structure enables identification of new proteins, and interpretation with molecular models highlights origins of new components, reveals modifications of the conserved motor core, and explain how these structures both template a wider ring of motor proteins, and buttress the motor during swimming reversals. We also acquire insights into universal principles of flagellar torque generation. This approach is broadly applicable to other membrane-residing bacterial molecular machines complexes. PubMed: 39416179DOI: 10.1101/2023.09.08.556779 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.9 Å) |
Structure validation
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