Structural features of the yeast plasma-membrane H(+)-ATPase.
The yeast plasma-membrane H(+)-ATPase is a member of the P-family of cation transporters, which share a characteristic membrane topology together with consensus sequences for ATP binding and formation of a beta-aspartyl phosphate reaction intermediate. Although direct knowledge of ATPase structure has been difficult to obtain, several indirect approaches have yielded useful information. This chapter describes new results on the physical interaction between domains of the yeast ATPase and on the role of cysteine residues in structure, function, and biogenesis. A model is proposed based upon these and other recent findings.
Padmanabha
K P
KP
Department of Genetics, Yale University School of Medicine, New Haven, CT 06510, USA.
Petrov
V
V
Ambesi
A
A
Rao
R
R
Slayman
C W
CW
D002462:Cell Membrane / Q000201:enzymology*; D003545:Cysteine / Q000378:metabolism; D008954:Models, Biological; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D006180:Proton-Translocating ATPases; D003545:Cysteine