A MOLECULAR SWITCH - SUBUNIT ROTATIONS INVOLVED IN THE RIGHT-HANDED TO LEFT-HANDED TRANSITIONS OF SALMONELLA-TYPHIMURIUM FLAGELLAR FILAMENTS

被引:34
作者
TRACHTENBERG, S [1 ]
DEROSIER, DJ [1 ]
机构
[1] BRANDEIS UNIV, ROSENSTIEL BASIC MED SCI RES CTR, WALTHAM, MA 02254 USA
关键词
CRYOELECTRON MICROSCOPY; BACTERIAL FLAGELLA; HELICAL 3-DIMENSIONAL RECONSTRUCTION; BACTERIAL MOTILITY; SWITCHABLE PROTEIN;
D O I
10.1016/0022-2836(91)90381-F
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using the combined techniques of cryoelectron microscopy and image analysis, we generated three-dimensional reconstructions of flagellar filaments from straight, right-handed (SJW1655-R) and straight, left-handed (SJW1660-L) Salmonella typhimurium mutants, both of which have the same parental strain (SJW1103). In the filaments from SJW1655, all flagellin subunits have the same conformation (R), while in filaments from SJW1660, the subunits are all in the alternate (L) conformation. The differences between the two three-dimensional density maps reveal the structural changes that accompany switching of the flagellin subunits between the two conformations. In going from the R to L state, the subunit undergoes a rotation 30 ° clockwise about a radial axis and 38 ° clockwise about a vertical axis, and suffers a 50 ° bend of the outer, relative to the inner, subunit domain. The intersubunit spacing, along the 11-start protofilaments, changes from 51·6 Å in the right-handed filament to 52·1 Å in the left-handed filament. In order to produce the correct corkscrew shape in native filaments, the change in contacts that produces this shortening of 0·5 Å must occur among the inner domains at a radius of about 30 Å. We suggest that the changes in the middle domains of the subunit are the switch that forces changes in the inner domains. © 1991.
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页码:67 / 77
页数:11
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