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...

Full description

Saved in:
Bibliographic Details
Published inJournal of structural biology Vol. 122; no. 3; pp. 311 - 319
Main Authors Khan, Shahid, Zhao, Rongbao, Reese, Thomas S.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 1998
Online AccessGet full text

Cover

More Information
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.
ISSN:1047-8477
1095-8657
DOI:10.1006/jsbi.1998.3999