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.
%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
}