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Biochim Biophys Acta. 2007 Nov;1767(11):1310-8. Epub 2007 Aug 16.

Proton paths in the sarcoplasmic reticulum Ca(2+) -ATPase.

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  • 1Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Svante Arrhenius väg 12, SE-106 91, Stockholm, Sweden.

Abstract

The sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) pumps Ca(2+) and countertransport protons. Proton pathways in the Ca(2+) bound and Ca(2+)-free states are suggested based on an analysis of crystal structures to which water molecules were added. The pathways are indicated by chains of water molecules that interact favorably with the protein. In the Ca(2+) bound state Ca(2)E1, one of the proposed Ca(2+) entry paths is suggested to operate additionally or alternatively as proton pathway. In analogs of the ADP-insensitive phosphoenzyme E2P and in the Ca(2+)-free state E2, the proton path leads between transmembrane helices M5 to M8 from the lumenal side of the protein to the Ca(2+) binding residues Glu-771, Asp-800 and Glu-908. The proton path is different from suggested Ca(2+) dissociation pathways. We suggest that separate proton and Ca(2+) pathways enable rapid (partial) neutralization of the empty cation binding sites. For this reason, transient protonation of empty cation binding sites and separate pathways for different ions are advantageous for P-type ATPases in general.

PMID:
17904096
DOI:
10.1016/j.bbabio.2007.07.010
[PubMed - indexed for MEDLINE]
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