Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Bacterial Proton-Translocating ATPases / chemistry*
-
Bacterial Proton-Translocating ATPases / genetics
-
Bacterial Proton-Translocating ATPases / metabolism
-
Binding Sites
-
Clostridium / enzymology*
-
Crystallization
-
Escherichia coli Proteins
-
Models, Molecular
-
Molecular Sequence Data
-
Protein Subunits / chemistry
-
Protein Subunits / genetics
-
Protein Subunits / metabolism
-
Protons
-
Sequence Alignment
-
Sodium / metabolism
-
Sodium Dodecyl Sulfate
Substances
-
Escherichia coli Proteins
-
Protein Subunits
-
Protons
-
atpE protein, E coli
-
Sodium Dodecyl Sulfate
-
Sodium
-
Bacterial Proton-Translocating ATPases