%0 Journal Article %1 Toyo_2004_269 %A Toyoshima, Chikashi %A Inesi, Giuseppe %D 2004 %J Annu. Rev. Biochem. %K 15189143 ATPase, Acid Adenosine Amino Animals, Binding Crystallography, Data, Gov't, Ion Models, Molecular Molecular, Muscle, Non-U.S. P.H.S., Phosphorylation, Protein Research Reticulum, Sarcoplasmic Sequence Sequence, Sites, Skeletal, Structure, Support, Tertiary, Transport, Triphosphate, U.S. X-Ray, {C}a$^{2+}$-Transporting %P 269--292 %R 10.1146/annurev.biochem.73.011303.073700 %T Structural basis of ion pumping by Ca$^2+$-ATPase of the sarcoplasmic reticulum. %U http://dx.doi.org/10.1146/annurev.biochem.73.011303.073700 %V 73 %X The structures of the Ca$^2+$-ATPase (SERCA1a) have been determined for five different states by X-ray crystallography. Detailed comparison of the structures in the Ca$^2+$ bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca$^2+$ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains as well as the mechanistic roles of phosphorylation are now becoming clear. Furthermore, the roles of critical amino acid residues identified by extensive mutagenesis studies are becoming evident in terms of atomic structure.

@article{Toyo_2004_269, abstract = {The structures of the {C}a$^{2+}$-ATPase (SERCA1a) have been determined for five different states by {X}-ray crystallography. Detailed comparison of the structures in the {C}a$^{2+}$ bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying {C}a$^{2+}$ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains as well as the mechanistic roles of phosphorylation are now becoming clear. Furthermore, the roles of critical amino acid residues identified by extensive mutagenesis studies are becoming evident in terms of atomic structure.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Toyoshima, Chikashi and Inesi, Giuseppe}, biburl = {https://www.bibsonomy.org/bibtex/28f5e79e5fd2b0bd3dcde824d67e6b0c4/hake}, description = {The whole bibliography file I use.}, doi = {10.1146/annurev.biochem.73.011303.073700}, file = {Toyo_2004_269.pdf:Toyo_2004_269.pdf:PDF}, interhash = {503e55c60e5939c84b0f9460a86c13b5}, intrahash = {8f5e79e5fd2b0bd3dcde824d67e6b0c4}, journal = {Annu. Rev. Biochem.}, key = 192, keywords = {15189143 ATPase, Acid Adenosine Amino Animals, Binding Crystallography, Data, Gov't, Ion Models, Molecular Molecular, Muscle, Non-U.S. P.H.S., Phosphorylation, Protein Research Reticulum, Sarcoplasmic Sequence Sequence, Sites, Skeletal, Structure, Support, Tertiary, Transport, Triphosphate, U.S. X-Ray, {C}a$^{2+}$-Transporting}, pages = {269--292}, pmid = {15189143}, timestamp = {2009-06-03T11:21:34.000+0200}, title = {Structural basis of ion pumping by {C}a$^{2+}$-ATPase of the sarcoplasmic reticulum.}, url = {http://dx.doi.org/10.1146/annurev.biochem.73.011303.073700}, volume = 73, year = 2004 }