Pumping ions

MacLennan, D H; Nm, Green

doi:10.1038/35015206

Cited by 58 publications

(39 citation statements)

References 13 publications

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“…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: 77%

“…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).…”

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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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confidence: 77%

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confidence: 99%

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

Liu

Barth

2003

Journal of Biological Chemistry

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“…The small actuator domain of the ATPase, its third cytoplasmic domain, is unique. As is the case for CheY and other receiver domains, the P domain of the intact Ca 2ϩ -ATPase can be phosphorylated by acetylphosphate rather than ATP (16,17,42), an activity that presumably does not depend on its N domain. Phosphorylation by either donor acts as a key switch during Ca 2ϩ transport (16,17,42).…”

Section: Fig 2 Ribbon Diagram Of Bef 3 ϫ ⅐Psp (A) and Stereoview Ofmentioning

confidence: 99%

“…The subgroup of P-type ATPases serves in transport of cations across biological membranes (15)(16)(17). Phosphoenzyme intermediates have been detected among the phosphotransferases of the HAD superfamily (14, 18 -20) and are known to form during the catalytic cycle of P-type ATPases (1,(15)(16)(17). In both cases, phosphorylation requires a divalent cation, normally Mg 2ϩ , and occurs at a conserved aspartate residue.…”

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confidence: 99%

“…For example, the phosphotransferase subgroup includes several phosphatases, among them phosphoserine phosphatase (PSP), and some phosphomutases. The subgroup of P-type ATPases serves in transport of cations across biological membranes (15)(16)(17). Phosphoenzyme intermediates have been detected among the phosphotransferases of the HAD superfamily (14, 18 -20) and are known to form during the catalytic cycle of P-type ATPases (1,(15)(16)(17).…”

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BeF\documentclass[12pt]{minimal}\usepackage{amsmath}\usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy}\usepackage{mathrsfs}\setlength{\oddsidemargin}{-69pt}\begin{document}\begin{equation}{\mathrm{_{3}^{-}}}\end{equation}\end{document} acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF\documentclass[12pt]{minimal}\usepackage{amsmath}\usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy}\usepackage{mathrsfs}\

Cho

Wang

Kim

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

123

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Calcium Signaling

Brini¹,

Fedrizzi²,

Carafoli³

2008

Wiley Encyclopedia of Chemical Biology

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Calcium is a universal second messenger that controls many cellular reactions. Considering its pleiotropic role, it seems evident that the cells, to get a specific message in the proper time and manner, need precise and efficient mechanisms to encode and decode Ca 2+ signals. Generally, extracellular stimuli are converted in a transient increase in cytosolic Ca 2+ concentration, [Ca 2+ ] c , which, in turn, modulates cell function. In the last two decades, improvements in the development of probes and instrumentation for Ca 2+ imaging have led to the discovery that the coordinated action of different players is responsible for a complex spatio‐temporal organization of the Ca 2+ signal. It is intriguing to observe that cells can encode and discriminate Ca 2+ signals not only according to their magnitude but also according to their localization (microdomains) and shape; i.e., cells can discriminate between sustained and oscillatory signals. Even more, in the case of oscillations, messages can be read differently according to the frequency of the oscillatory signals. The mechanisms by which cells decode Ca 2+ signals are now explored in numerous laboratories. This article focuses on the autoregulation properties of the Ca 2+ signals. It will show that Ca 2+ itself is central in the regulation of the Ca 2+ signal. It will also show that it can act as a first and second messenger and that it can modulate the activity and the availability of the other players in the signaling operation.

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Pumping ions

Cited by 58 publications

References 13 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 Signaling

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