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Proteolytic Studies on the Transduction Mechanism of Sarcoplasmic Reticulum Ca2+-ATPase
| Content Provider | Scilit |
|---|---|
| Author | Møller, Jesper V. Lenoir, Guillaume Maire, Marc Juul, Birte Staehr Champeil, Philippe |
| Copyright Year | 2003 |
| Description | Journal: Annals of the New York Academy of Sciences After proteinase K-induced excision of five amino acid residues in the semiconserved polypeptide chain linking the end of the A domain with the S3/M3 transmembrane segment we find that Ca(2+) transport is blocked while partial reactions like Ca(2+) binding, ATP phosphorylation, and Ca(2+)-occlusion are left intact. However, formation of the so-called E2P state (either from the phosphorylated species formed in the presence of ATP and Ca(2+) or from the Ca(2+)-depleted unphosphorylated species) is blocked. We conclude that the proteinase K-treated ATPase, while maintaining many of the partial reactions, is incapable of energy transduction because of the absence of an E2P state with Ca(2+) binding sites exposed to the intravesicular space. Sequence comparisons and mutagenesis data point to an important role in energy transduction of P-type ATPases of a conserved motif located at the end of the A domain. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.2003.tb07142.x/pdf |
| Ending Page | 89 |
| Page Count | 8 |
| Starting Page | 82 |
| e-ISSN | 17496632 |
| DOI | 10.1111/j.1749-6632.2003.tb07142.x |
| Journal | Annals of the New York Academy of Sciences |
| Issue Number | 1 |
| Volume Number | 986 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2003-04-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Annals of the New York Academy of Sciences Biochemistry and Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
