| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2031366 | Trends in Biochemical Sciences | 2008 | 5 Pages |
Abstract
Cation-transporting P-type ATPases show a high degree of structural and functional homology. Nevertheless, for many members of this large family, the molecular mechanism of transport is unclear; namely, whether transport is electrogenic or not and if countertransport is involved remains to be established. In a few well-studied cases such as the Na+–K+-ATPase, plasma membrane Ca2+ ATPase (PMCA) and sarcoplasmic reticulum Ca2+ ATPase (SERCA) countertransport has been clearly demonstrated. New data based on the crystal structure of SERCA now strongly indicate that countertransport could be mandatory for all P-type ATPases. This concept should be verified for other known and for all newly characterized P-type ATPases.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Verena Niggli, Erwin Sigel,