Structural features of the yeast plasma-membrane H(+)-ATPase.

K. P. Padmanabha, V. Petrov, A. Ambesi, R. Rao, C. W. Slayman

Research output: Contribution to journalReview article

Abstract

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.

Original languageEnglish (US)
Pages (from-to)33-42
Number of pages10
JournalSymposia of the Society for Experimental Biology
Volume48
StatePublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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