TY - JOUR
T1 - Architectural features of the Salmonella typhimurium flagellar motor switch revealed by disrupted C-rings
AU - Khan, Shahid
AU - Zhao, Rongbao
AU - Reese, Thomas S.
N1 - Funding Information:
We thank Jennifer Peterson for expert technical assistance. Supported, in part, by Grant GM36936 from the National Institutes of Health.
PY - 1998
Y1 - 1998
N2 - The three-dimensional surface topology of rapid-frozen Salmonella typhimurium flagellar 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.
AB - The three-dimensional surface topology of rapid-frozen Salmonella typhimurium flagellar 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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U2 - 10.1006/jsbi.1998.3999
DO - 10.1006/jsbi.1998.3999
M3 - Article
C2 - 9774535
AN - SCOPUS:0031684602
SN - 1047-8477
VL - 122
SP - 311
EP - 319
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 3
ER -