P-type ion transporting ATPases are ATP-powered ion pumps that establish
ion concentration gradients across biological membranes. Transfer
of bound cations to the lumenal or extracellular side occurs while
the ATPase is phosphorylated. Here we report at 2.3 A resolution
the structure of the calcium-ATPase of skeletal muscle sarcoplasmic
reticulum, a representative P-type ATPase that is crystallized in
the absence of Ca$^2+$ but in the presence of magnesium fluoride,
a stable phosphate analogue. This and other crystal structures determined
previously provide atomic models for all four principal states in
the reaction cycle. These structures show that the three cytoplasmic
domains rearrange to move six out of ten transmembrane helices, thereby
changing the affinity of the Ca$^2+$-binding sites and the gating
of the ion pathway. Release of ADP triggers the opening of the
lumenal gate and release of phosphate its closure, effected mainly
through movement of the A-domain, the actuator of transmembrane gates.
%0 Journal Article
%1 Toyo_2004_361
%A Toyoshima, Chikashi
%A Nomura, Hiromi
%A Tsuda, Takeo
%D 2004
%J Nature
%K 15549083 ATPase, Adenosine Binding Calcium, Catalysis, Channel Compounds, Crystallization, Crystallography, Diphosphate, Fluorides, Gating, Gov't, Ion Magnesium Models, Molecular, Non-U.S. Phosphates, Phosphorylation, Protein Relationship, Research Reticulum, Sarcoplasmic Secondary, Sites, Structure, Structure-Activity Support, Tertiary, Triphosphate, X-Ray, {C}a$^{2+}$-Transporting
%N 7015
%P 361--368
%R 10.1038/nature02981
%T Lumenal gating mechanism revealed in calcium pump crystal structures
with phosphate analogues.
%U http://dx.doi.org/10.1038/nature02981
%V 432
%X P-type ion transporting ATPases are ATP-powered ion pumps that establish
ion concentration gradients across biological membranes. Transfer
of bound cations to the lumenal or extracellular side occurs while
the ATPase is phosphorylated. Here we report at 2.3 A resolution
the structure of the calcium-ATPase of skeletal muscle sarcoplasmic
reticulum, a representative P-type ATPase that is crystallized in
the absence of Ca$^2+$ but in the presence of magnesium fluoride,
a stable phosphate analogue. This and other crystal structures determined
previously provide atomic models for all four principal states in
the reaction cycle. These structures show that the three cytoplasmic
domains rearrange to move six out of ten transmembrane helices, thereby
changing the affinity of the Ca$^2+$-binding sites and the gating
of the ion pathway. Release of ADP triggers the opening of the
lumenal gate and release of phosphate its closure, effected mainly
through movement of the A-domain, the actuator of transmembrane gates.
@article{Toyo_2004_361,
abstract = {P-type ion transporting ATPases are ATP-powered ion pumps that establish
ion concentration gradients across biological membranes. Transfer
of bound cations to the lumenal or extracellular side occurs while
the ATPase is phosphorylated. Here we report at 2.3 A resolution
the structure of the calcium-ATPase of skeletal muscle sarcoplasmic
reticulum, a representative P-type ATPase that is crystallized in
the absence of {C}a$^{2+}$ but in the presence of magnesium fluoride,
a stable phosphate analogue. This and other crystal structures determined
previously provide atomic models for all four principal states in
the reaction cycle. These structures show that the three cytoplasmic
domains rearrange to move six out of ten transmembrane helices, thereby
changing the affinity of the {C}a$^{2+}$-binding sites and the gating
of the ion pathway. Release of {ADP} triggers the opening of the
lumenal gate and release of phosphate its closure, effected mainly
through movement of the A-domain, the actuator of transmembrane gates.},
added-at = {2009-06-03T11:20:58.000+0200},
author = {Toyoshima, Chikashi and Nomura, Hiromi and Tsuda, Takeo},
biburl = {https://www.bibsonomy.org/bibtex/2998fe7dccc55b64408dac5e7ba1aa101/hake},
description = {The whole bibliography file I use.},
doi = {10.1038/nature02981},
file = {Toyo_2004_361.pdf:Toyo_2004_361.pdf:PDF},
interhash = {f48dba489d5d11b979f43fc0e5a0bf0d},
intrahash = {998fe7dccc55b64408dac5e7ba1aa101},
journal = {Nature},
key = 193,
keywords = {15549083 ATPase, Adenosine Binding Calcium, Catalysis, Channel Compounds, Crystallization, Crystallography, Diphosphate, Fluorides, Gating, Gov't, Ion Magnesium Models, Molecular, Non-U.S. Phosphates, Phosphorylation, Protein Relationship, Research Reticulum, Sarcoplasmic Secondary, Sites, Structure, Structure-Activity Support, Tertiary, Triphosphate, X-Ray, {C}a$^{2+}$-Transporting},
month = Nov,
number = 7015,
pages = {361--368},
pii = {nature02981},
pmid = {15549083},
timestamp = {2009-06-03T11:21:34.000+0200},
title = {Lumenal gating mechanism revealed in calcium pump crystal structures
with phosphate analogues.},
url = {http://dx.doi.org/10.1038/nature02981},
volume = 432,
year = 2004
}