Crystal structure of the calcium pump with a bound ATP analogue
@article{Toyoshima2004CrystalSO, title={Crystal structure of the calcium pump with a bound ATP analogue}, author={Chikashi Toyoshima and Tatsuaki Mizutani}, journal={Nature}, year={2004}, volume={430}, pages={529-535} }
P-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across cell and organelle membranes. Here, we describe the crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic reticulum, a representative member of the P-type ATPase superfamily, with an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites. In this state, the ATP analogue reorganizes the three cytoplasmic domains (A, N and P), which are widely separated without nucleotide, by…
426 Citations
Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
- Biology, ChemistryNature
- 2004
These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway.
The structural basis of calcium transport by the calcium pump
- Biology, ChemistryNature
- 2007
Functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase are presented, representing the phosphoenzyme intermediates associated withCa2+ binding, Ca2- translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively.
Crystal structure of the sodium–potassium pump at 2.4 Å resolution
- Biology, ChemistryNature
- 2009
The crystal structure shows that the β-subunit has a critical role in K+ binding (although its involvement has previously been suggested) and explains, at least partially, why the homologous Ca2+-ATPase counter-transports H+ rather than K+, despite the coordinating residues being almost identical.
Crystal structure of the plasma membrane proton pump
- BiologyNature
- 2007
The first structure of a P-type proton pump determined by X-ray crystallography is presented, and the structure is locked in a functional state not previously observed in P- type ATPases.
Modulatory and catalytic modes of ATP binding by the calcium pump
- Biology, ChemistryThe EMBO journal
- 2006
A mechanism of Ca2+ activation of phosphorylation leading directly from the compact E2‐ATP form to the Ca2E1‐ATp state is proposed and a role of Glu439 in ATP modulation of other steps of the functional cycle is suggested.
Transport mechanism of the sarcoplasmic reticulum Ca2+ -ATPase pump.
- Biology, ChemistryCurrent opinion in structural biology
- 2005
The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump
- Biology, ChemistryQuarterly Reviews of Biophysics
- 2010
The detailed construction of the ATPase is described in terms of one membraneous and three cytosolic domains held together by a central core that mediates coupling between Ca2+-transport and ATP hydrolysis and the role of the lipid phase and the regulatory and thermodynamic aspects of the transport mechanism are reviewed.
Crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) from bovine muscle.
- BiologyJournal of structural biology
- 2012
Structural Basis for the Function of the C-Terminal Proton Release Pathway in the Calcium Pump
- BiologyInternational journal of molecular sciences
- 2021
Calcium pump atomistic simulations demonstrate that in the protonated E2 state and the absence of initially bound water molecules, the C-terminal pore becomes hydrated in the nanosecond timescale and support the notion that the C.terminal proton release pathway is a functional element of SERCA and provide a mechanistic model for its operation in the catalytic cycle of the pump.
Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2013
A model for the ion exchange mechanism in PII-ATPases including not one, but two cytoplasmic pathways working in concert is suggested.
References
SHOWING 1-10 OF 61 REFERENCES
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
- Biology, ChemistryNature
- 2000
Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.
Structural changes in the calcium pump accompanying the dissociation of calcium
- BiologyNature
- 2002
The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca2+.
A structural model for the catalytic cycle of Ca(2+)-ATPase.
- Biology, ChemistryJournal of molecular biology
- 2002
It is hypothesized that both the nucleotide-binding and beta-sheet domains are highly mobile and driven by Brownian motion to elicit phosphoenzyme formation and calcium transport, respectively, and the reaction cycle of Ca(2+)-ATPase would have elements of a Brownian ratchet.
ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase
- Biology, ChemistryNature Structural Biology
- 2003
Two high-resolution NMR structures are reported of the 213-residue nucleotide-binding domain of rat α1 Na,K-ATPase, determined in the absence and the presence of ATP, showing the low-affinity ATP-binding state.
The ATP Binding Sites of P-Type ION Transport ATPases: Properties, Structure, Conformations, and Mechanism of Energy Coupling
- Biology, Chemistry
- 1997
Structural basis of ion pumping by Ca2+‐ATPase of sarcoplasmic reticulum
- BiologyAnnual review of biochemistry
- 2004
Substrate-induced Conformational Fit and Headpiece Closure in the Ca2+ATPase (SERCA)*
- Biology, ChemistryJournal of Biological Chemistry
- 2003
By mutational analysis the protective effect of AMP-PCP, an ATP analog that is not utilized for enzyme phosphorylation, is studied and it is found that the nucleotide protective effect is interfered with by single mutations of Arg-560 and Glu-439 in the N domain and Lys-352, Lys-684, Thr-353, Asp-703, and Asn-706 to Ala.
Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2003
The conformation of the first phosphorylated ATPase intermediate E1PCa2 also depends on the nucleotide, indicating that ATPase states have a less uniform conformation than previously anticipated.
Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms.
- Biology, ChemistryBiochemistry
- 1998
The functional consequences of mutations Glu329 --> Gln in the Na+,K+-ATPase and Glu309 --> Asp in the sarco(endo)plasmic reticulum Ca2+-ATPase were analyzed and compared. Relative to the wild-type…
Nucleotide binding by the histidine kinase CheA
- Biology, ChemistryNature Structural Biology
- 2001
The crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs bound with either Mg2+ or Mn2+.