Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy

• Published in: Biochemistry (Easton) Vol. 29; no. 22; pp. 5339 - 5343
• Main Authors: Luecken, Uwe, Gogol, Edward P, Capaldi, Roderick A
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 05-06-1990
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Cryopreservation; Enzymes and enzyme inhibitors; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; Hydrolases; Microscopy, Electron; Proton-Translocating ATPases - ultrastructure; ATP-synthase complex; Image analysis; Molecular structure; Enzyme; Escherichia coli; Reconstituted system; Bacteria; Biomembrane; Electron microscopy; Enterobacteriaceae
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00474a019

The structural relationship of the catalytic portion (ECF1) of the Escherichia coli F1F0 ATP synthase (ECF1F0) to the intact, membrane-bound complex has been determined by cryoelectron microscopy and image analysis of single, unordered particles. ECF1F0, reconstituted into membrane structures, has been preserved and examined in its native state in a layer of amorphous ice. Side views of the ECF1F0 show the same elongated bilobed and trilobed projection of the ECF1 views shown previously to be normal to the hexagonal projection. The elongated aqueous cavity of the ECF1 is perpendicular to the membrane bilayer profile in the bilobed view. ECF1 is separated from the membrane-embedded F0 by a narrow stalk approximately 40 A long and approximately 25-30 A thick. The F0 part extends from the lipid bilayer by approximately 10 A on the side facing the ECF1. There is no clear extension of the protein on the opposite side of the membrane.