Molecular polarity in tropomyosin troponin T co-crystals

被引:34
作者
CabralLilly, D
Tobacman, LS
Mehegan, JP
Cohen, C
机构
[1] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254
[2] UNIV IOWA,COLL MED,DEPT INTERNAL MED,IOWA CITY,IA 52242
关键词
D O I
10.1016/S0006-3495(97)78206-7
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
New features of the structure and interactions of troponin T and tropomyosin have been revealed by electron microscopy of so-called double-diamond co-crystals. These co-crystals were formed using rabbit alpha(2) tropomyosin complexed with troponin T from either skeletal or cardiac muscle, which have different lengths in the amino-terminal region, as well as a bacterially expressed skeletal muscle troponin T fragment of 190 residues that lacks the amino-terminal region. Differences in the images of the co-crystals have allowed us to establish the polarities of both the troponin T subunit and tropomyosin in the projected lattice. Moreover, in agreement with their sequences, the amino-terminal region of a bovine cardiac muscle troponin T isoform appears to be longer than that from the rabbit skeletal muscle troponin T isoform and to span more of the amino terminus of tropomyosin at the head-to-tail filament joints. Images of crystals tilted relative to the electron beam also reveal the supercoiling of the tropomyosin filaments in this lattice. Based on these results, a three-dimensional model of the double-diamond lattice has been constructed.
引用
收藏
页码:1763 / 1770
页数:8
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