Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum.
The Na(+)-translocating F-ATPase of the thermoalkaliphilic bacterium Clostridium paradoxum harbors an oligomeric ring of c subunits that resists dissociation by sodium dodecyl sulfate. The c ring has been isolated and crystallized in two dimensions. From electron microscopy of these c-ring crystals, a projection map was calculated to 7 A resolution. In the projection map, each c ring consists of two concentric, slightly staggered, packed rings, each composed of 11 densities representing the alpha-helices. On the basis of these results, it was determined that the F-ATPase from C. paradoxum contains an undecameric c ring.
Meier
Thomas
T
Max-Planck-Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt, Germany. thomas.meier@mpibp-frankfurt.mpg.de
Ferguson
Scott A
SA
Cook
Gregory M
GM
Dimroth
Peter
P
Vonck
Janet
J
D000595:Amino Acid Sequence; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011522:Protons; D016415:Sequence Alignment; D012964:Sodium / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate
D029968:Escherichia coli Proteins; D021122:Protein Subunits; D011522:Protons; C074429:atpE protein, E coli; D012967:Sodium Dodecyl Sulfate; D012964:Sodium; D025243:Bacterial Proton-Translocating ATPases