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9N4Z

CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring from Salmonella

This is a non-PDB format compatible entry.
Replaces:  8T8O
Summary for 9N4Z
Entry DOI10.2210/pdb9n4z/pdb
Related9N49
EMDB information48916
DescriptorFlagellar M-ring protein, Flagellar motor switch protein FliG, Flagellar motor switch protein FliM, ... (4 entities in total)
Functional Keywordsc-ring, bacterial, chemotaxis, c ring, flagellar motor complex, switch complex, flig, flim, flin, flif, motor protein
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
More
Total number of polymer chains204
Total formula weight6136766.66
Authors
Singh, P.K.,Iverson, T.M. (deposition date: 2025-02-03, release date: 2025-03-19, Last modification date: 2025-04-02)
Primary citationSingh, P.K.,Iverson, T.M.
Improving CryoEM maps of symmetry-mismatched macromolecular assemblies: A case study on the flagellar motor.
J.Struct.Biol., 217:108184-108184, 2025
Cited by
PubMed Abstract: Advances in cryo-electron microscopy instrumentation and sample preparation have significantly improved the ability to collect quality data for biomolecular structures. However, achieving resolutions consistent with data quality remains challenging in structures with symmetry mismatches. As a case study, the bacterial flagellar motor is a large complex essential for bacterial chemotaxis and virulence. This motor contains a smaller membrane-supramembrane ring (MS-ring) and a larger cytoplasmic ring (C-ring). These two features have a 33:34 symmetry mismatch when expressed in E. coli. Because close symmetry mismatches are the most difficult to deconvolute, this makes the flagellar motor an excellent model system to evaluate refinement strategies for symmetry mismatch. We compared the performance of masked refinement, local refinement, and particle subtracted refinement on the same data. We found that particle subtraction prior to refinement was essential for correctly deconvoluting the symmetry of the smaller MS-ring. Additional processing resulted in final resolutions of 3.1 Å for the MS-ring and 3.0 Å for the C-ring, which improves the resolution of the MS-ring by 0.3 Å and the resolution of the C-ring by 1.0 Å as compared to past work. Although particle subtraction is fairly well-established, it is rarely applied to problems of symmetry mismatch, making this case study a valuable demonstration of its utility in this context.
PubMed: 40054642
DOI: 10.1016/j.jsb.2025.108184
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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PDB entries from 2025-04-16

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