Architectural Features of theSalmonella typhimuriumFlagellar Motor Switch Revealed by Disrupted C-Rings
The three-dimensional surface topology of rapid-frozenSalmonella typhimuriumflagellar hook basal body complexes was studied by stereo-examination of thin-film metal replicas. The complexes contained the extended cytoplasmic structure, composed of the switch complex proteins; FliG, FliM, and FliN. Di...
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Published in | Journal of structural biology Vol. 122; no. 3; pp. 311 - 319 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
1998
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Online Access | Get full text |
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Summary: | The three-dimensional surface topology of rapid-frozenSalmonella typhimuriumflagellar hook basal body complexes was studied by stereo-examination of thin-film metal replicas. The complexes contained the extended cytoplasmic structure, composed of the switch complex proteins; FliG, FliM, and FliN. Distinct nanometer-scale element arrays, separated by grooves, defined the outer surface of the cytoplasmic (C-) ring. The number of array elements was comparable to previously determined FliG and FliM copy numbers in the basal body. In addition to basal body complexes lacking C-rings, complexes containing incomplete C-rings were identified. The incomplete C-rings had lost segments of the proximal array. Basal bodies with the distal C-ring array alone were not found. These findings are compatible with the spatial organization of the flagellar switch suggested by previous biochemical data. |
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ISSN: | 1047-8477 1095-8657 |
DOI: | 10.1006/jsbi.1998.3999 |