Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+‐ATPase in E1P and E1ATP states: a limited proteolysis study

Dankó, Stefánia; Yamasaki, Kazuo; Daiho, Takashi; Suzuki, Hiroshi; Toyoshima, Chikashi

doi:10.1016/s0014-5793(01)02801-0

Cited by 96 publications

(131 citation statements)

References 49 publications

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“…Our finding of a nucleotide specific conformation of the nucleotide-ATPase complexes is supported by previous reports, in which different effects of different nucleotides were found on fluorescence properties (17,18,53), partial reaction rates (54 -57), protection against proteolysis (21), effects of aromatic compounds (58), nucleotide binding properties of mutants (25), and uncoupling (59).…”

Section: Discussionsupporting

confidence: 90%

“…The latter does not seem to contribute to a large extent to our spectra for the following reason: Danko et al (21) studied protection of the ATPase against proteolytic attack by various nucleotides. This effect is thought to reflect a movement of the A-domain.…”

Section: Discussionmentioning

confidence: 99%

“…The Conformational Change Reflected in IR Spectra-Conformational changes in two regions of the protein were proposed to occur upon nucleotide binding (21): (i) movement of the N-domain toward the P-domain and (ii) movement of the A-domain toward the P-domain. The latter does not seem to contribute to a large extent to our spectra for the following reason: Danko et al (21) studied protection of the ATPase against proteolytic attack by various nucleotides.…”

Section: Discussionmentioning

confidence: 99%

“…The structure has been solved with and without 2Ј,3Ј-O-(2,4,6-trinitrophenyl)adenosine 5Ј-monophosphate (TNP-AMP), which binds to the N-domain at considerable distance from the phosphorylation site Asp 351 with less structural effects than ATP (20,21). ATP is thought to bind to the surface of the N-domain with the phosphate groups pointing toward the phosphorylation site Asp 351 (21), and most of the residues associated with the nucleotide binding site are located in the N-domain (12, 16, 20 -24). Closure of the cleft between N-and P-domain is thought to occur to bring ATP close to Asp 351 upon nucleotide binding (20,21).…”

mentioning

confidence: 99%

“…ATP is thought to bind to the surface of the N-domain with the phosphate groups pointing toward the phosphorylation site Asp 351 (21), and most of the residues associated with the nucleotide binding site are located in the N-domain (12, 16, 20 -24). Closure of the cleft between N-and P-domain is thought to occur to bring ATP close to Asp 351 upon nucleotide binding (20,21). In line with that, mutations at Asp 351 , Lys 352 (25), and Thr 353 (26) alter the affinity of ATP to the ATPase.…”

mentioning

confidence: 99%

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Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy

Liu

Barth

2003

Journal of Biological Chemistry

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Infrared spectroscopy has been used to map substrate-protein interactions: the conformational changes of the sarcoplasmic reticulum Ca 2؉ -ATPase upon nucleotide binding and ATPase phosphorylation were monitored using the substrate ATP and ATP analogues (2 -deoxy-ATP, 3 -deoxy-ATP, and inosine 5 -triphosphate), which were modified at specific functional groups of the substrate. Modifications to the 2 -OH, the 3 -OH, and the amino group of adenine reduce the extent of bindinginduced conformational change of the ATPase, with particularly strong effects observed for the latter two. This demonstrates the structural sensitivity of the nucleotide-ATPase complex to individual interactions between nucleotide and ATPase. All groups studied are important for binding and interactions of a given ligand group with the ATPase depend on interactions of other ligand groups.Phosphorylation of the ATPase was observed for ITP and 2 -deoxy-ATP, but not for 3 -deoxy-ATP. There is no direct link between the extent of conformational change upon nucleotide binding and the rate of phosphorylation showing that the full extent of the ATP-induced conformational change is not mandatory for phosphorylation. As observed for the nucleotide-ATPase complex, the conformation of the first phosphorylated ATPase intermediate E1PCa 2 also depends on the nucleotide, indicating that ATPase states have a less uniform conformation than previously anticipated.Ligand binding to proteins controls vast numbers of cellular processes and has attracted great scientific and economic interest. Protein and ligand flexibility are important determinants of the interaction and often lead to ligand binding modes that are not anticipated from structures obtained with other ligands. To these "failure(s) of the rigid receptor hypothesis" (1) is added here an impressive example: induced-fit binding of nucleotides to the Ca 2ϩ -ATPase. This finding stems from a systematic mapping of substrate-protein interactions with infrared (IR) 1 spectroscopy. New approaches like this are welcome in the field of ligand-protein recognition, since the most informative techniques, NMR and x-ray crystallography, are laborious and problematic for some systems. Methods like fluorescence and luminescence that require less expenditure also provide less molecular information. We expect that this technology gap will be bridged by IR spectroscopy.IR spectroscopy, one of the methods of vibrational spectroscopy, provides direct information on the molecular level, is cost-effective, and can be universally applied from small soluble proteins to large membrane proteins under near-physiological conditions. Work summarized in recent reviews (2-5) has shown that the vibrational spectrum changes characteristically when a ligand binds to a protein. This provides a direct observation of ligand binding: no marker compound has to be introduced to report the binding process, as with many other methods. Previous work has mostly focused on individual interactions between a ligand and a protein by monitoring the ...

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy

Liu

Barth

2003

Journal of Biological Chemistry

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Calcium Pump ( ATPase ) of Sarcoplasmic Reticulum

Toyoshima¹

2004

Handbook of Metalloproteins

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Ca 2+ ‐ATPase of sarcoplasmic reticulum is a membrane protein of 110 kDa and pumps Ca 2+ from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle, to relax muscle cells. Two Ca 2+ ions can be transported per ATP hydrolyzed and two or three protons are countertransported. The Ca 2+ ‐binding sites are located side by side in the transmembrane region. The crystal structures of this ATPase obtained for Ca 2+ ‐bound and unbound states show that large conformation changes take place during Ca 2+ binding and dissociation.

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ATPase reaction cycle of P4‐ATPases affects their transport from the endoplasmic reticulum

et al. 2019

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P4‐ATPases belonging to the P‐type ATPase superfamily mediate active transport of phospholipids across cellular membranes. Most P4‐ATPases, except ATP9A and ATP9B proteins, form heteromeric complexes with CDC50 proteins, which are required for transport of P4‐ATPases from the endoplasmic reticulum (ER) to their final destinations. P‐type ATPases form autophosphorylated intermediates during the ATPase reaction cycle. However, the association of the catalytic cycle of P4‐ATPases with their transport from the ER and their cellular localization has not been studied. Here, we show that transport of ATP9 and ATP11 proteins as well as that of ATP10A from the ER depends on the ATPase catalytic cycle, suggesting that conformational changes in P4‐ATPases during the catalytic cycle are crucial for their transport from the ER.

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Organization of cytoplasmic domains of sarcoplasmic reticulum Ca²⁺‐ATPase in E₁P and E₁ATP states: a limited proteolysis study

Cited by 96 publications

References 49 publications

Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy

Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy

Calcium Pump ( ATPase ) of Sarcoplasmic Reticulum

ATPase reaction cycle of P4‐ATPases affects their transport from the endoplasmic reticulum

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