The structure of the H(+)-ATP synthase from chloroplasts and its subcomplexes as revealed by electron microscopy.
The electron microscopic data available on CF(0)F(1) and its subcomplexes, CF(0), CF(1), subunit III complex are collected and the CF(1) data are compared with the high resolution structure of MF(1). The data are based on electron microscopic investigation of negatively stained isolated CF(1), CF(0)F(1) and subunit III complex. In addition, two-dimensional crystals of CF(0)F(1) and CF(0)F(1) reconstituted liposomes were investigated by cryo-electron microscopy. Progress in the interpretation of electron microscopic data from biological samples has been made with the introduction of image analysis. Multi-reference alignment and classification of images have led to the differentiation between different conformational states and to the detection of a second stalk. Recently, the calculation of three-dimensional maps from the class averages led to the understanding of the spatial organisation of the enzyme. Such three-dimensional maps give evidence of the existence of a third connection between the F(0) part and F(1) part.
Böttcher
B
B
European Molecular Biology Laboratory, Heidelberg, Germany.
Gräber
P
P
D002736:Chloroplasts / Q000201:enzymology*; D020285:Cryoelectron Microscopy; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D011510:Proteolipids / Q000648:ultrastructure; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000648:ultrastructure; D014961:X-Ray Diffraction
D011510:Proteolipids; C020485:proteoliposomes; D006180:Proton-Translocating ATPases