We have used the 2.6 Å structure of the rabbit sarcoplasmic reticulum Ca2+-ATPase isoform 1a, SERCA1a [Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. (2000) Nature 405, 647-655], to build models by homology modelling of two plasma membrane (PM) H+-ATPases, Arabidopsis thaliana AHA2 and Saccharomyces cerevisiae PMA1. We propose that in both yeast and plant PM H+-ATPases a strictly conserved aspartate in transmembrane segment (M)6 (D684AHA2/D730PMA1), and three backbone carbonyls in M4 (I282AHA2/I331PMA1, G283AHA2/I332PMA1 and I285AHA2/V334PMA1) comprise a binding site for H3O+, suggesting a previously unknown mechanism for transport of protons. Comparison with the structure of the SERCA1a made it feasible to suggest a possible receptor region for the C-terminal auto-inhibitory domain extending from the phosphorylation and anchor domains into the transmembrane region. © 2001 Federation of European Biochemical Societies.
Bukrinsky, J. T., Buch-Pedersen, M. J., Larsen, S., & Palmgren, M. G. (2001). A putative proton binding site of plasma membrane H+-ATPase identified through homology modelling. FEBS Letters, 494(1–2), 6–10. https://doi.org/10.1016/S0014-5793(01)02301-8