3-DIMENSIONAL CRYOELECTRON MICROSCOPY OF THE CALCIUM-ION PUMP IN THE SARCOPLASMIC-RETICULUM MEMBRANE

被引:207
作者
TOYOSHIMA, C
SASABE, H
STOKES, DL
机构
[1] UNIV VIRGINIA, HLTH SCI CTR,DEPT MOLEC PHYSIOL & BIOL PHYS, JORDAN HALL,BOX 449, CHARLOTTESVILLE, VA 22908 USA
[2] TOKYO INST TECHNOL, DEPT BIOL SCI, MEGURO KU, TOKYO 152, JAPAN
[3] RIKEN, FRONTIER RES PROGRAM, WAKO, SAITAMA 35101, JAPAN
关键词
D O I
10.1038/362469a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
THE ATP-driven calcium pump (Ca2+-ATPase) is an integral membrane protein (M(r) 110K) which relaxes striated muscle by pumping calcium out of the cytoplasm into the sarcoplasmic reticulum against a large concentration gradient1. Recent efforts have attempted to relate the sequence of Ca2+-ATPase to its structure and function. In particular, site-directed mutagenesis has identified critical amino-acid residues2-6, and its predicted secondary structure, which includes ten transmembrane helices7, has gained experimental support8-10. But direct visualization of the molecule has so far been limited to the cytoplasmic domains at low resolution11,12. We present here the three-dimensional structure of Ca2+-ATPase in the native sarcoplasmic reticulum membrane at 14 angstrom resolution, determined by cryo-electron microscopy and helical image analysis. The structure shows an unexpected transmembrane organization, consisting of three distinct segments, one of which is highly inclined. These features can be related to earlier predictions of secondary structure.
引用
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页码:469 / 471
页数:3
相关论文
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