E1/E2 type cation transport ATPases: evidence for transient associations between protomers.
E1/E2 type cation transport ATPases are known to exist in different conformeric states. Recent evidence characterizing these conformers in membrane is reviewed. A consensus view is proposed in which E2 conformers tend to form oligomeric complexes by lateral association between monomeric protomers and E1 conformers exhibit the opposite behaviour. It is suggested that transient associations between monomers during cation pump cycles may be a common feature of the ion translocation mechanism under physiological conditions.
Boldyrev
A A
AA
Biotechnological Center of M. V. Lomonosov Moscow State University, Russia.
Quinn
P J
PJ
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D017136:Ion Transport; D011487:Protein Conformation; D012519:Sarcoplasmic Reticulum / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000378:metabolism*
D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase