Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis.
F- and V-type ATPases are central enzymes in energy metabolism that couple synthesis or hydrolysis of ATP to the translocation of H+ or Na+ across biological membranes. They consist of a soluble headpiece that contains the catalytic sites and an integral membrane-bound part that conducts the ion flow. Energy coupling is thought to occur through the physical rotation of a stalk that connects the two parts of the enzyme complex. This mechanism implies that a stator-like structure prevents the rotation of the headpiece relative to the membrane-bound part. Such a structure has not been observed to date. Here, we report the projected structure of the V-type Na+-ATPase of Clostridium fervidus as determined by electron microscopy. Besides the central stalk, a second stalk of 130 A in length is observed that connects the headpiece and membrane-bound part in the periphery of the complex. This additional stalk is likely to be the stator.
Boekema
E J
EJ
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen, The Netherlands. boekema@chem.rug.nl
Ubbink-Kok
T
T
Lolkema
J S
JS
Brisson
A
A
Konings
W N
WN
D003013:Clostridium / Q000201:enzymology*; D008854:Microscopy, Electron; D008958:Models, Molecular; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000648:ultrastructure; D025262:Vacuolar Proton-Translocating ATPases
D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases