Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR

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Standard

Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR. / Vostrikov, Vitaly V; Gustavsson, Martin; Gopinath, Tata; Mullen, Dan; Dicke, Alysha A; Truong, Vincent; Veglia, Gianluigi.

I: ACS chemical biology, Bind 11, Nr. 2, 19.02.2016, s. 329-34.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Vostrikov, VV, Gustavsson, M, Gopinath, T, Mullen, D, Dicke, AA, Truong, V & Veglia, G 2016, 'Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR', ACS chemical biology, bind 11, nr. 2, s. 329-34. https://doi.org/10.1021/acschembio.5b00953

APA

Vostrikov, V. V., Gustavsson, M., Gopinath, T., Mullen, D., Dicke, A. A., Truong, V., & Veglia, G. (2016). Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR. ACS chemical biology, 11(2), 329-34. https://doi.org/10.1021/acschembio.5b00953

Vancouver

Vostrikov VV, Gustavsson M, Gopinath T, Mullen D, Dicke AA, Truong V o.a. Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR. ACS chemical biology. 2016 feb. 19;11(2):329-34. https://doi.org/10.1021/acschembio.5b00953

Author

Vostrikov, Vitaly V ; Gustavsson, Martin ; Gopinath, Tata ; Mullen, Dan ; Dicke, Alysha A ; Truong, Vincent ; Veglia, Gianluigi. / Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR. I: ACS chemical biology. 2016 ; Bind 11, Nr. 2. s. 329-34.

Bibtex

@article{a133364d6e5e4161844920f821669dfd,
title = "Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR",
abstract = "To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by NMR at atomic resolution has been challenging due to the large size of these systems. It is further exacerbated for large mammalian proteins that are difficult to express and label with NMR-active isotopes. Here, we synthesized and engineered (13)C ethyl groups on native cysteines to map the structural transitions of the sarcoplasmic reticulum Ca(2+)-ATPase, a 110 kDa transmembrane enzyme that transports Ca(2+) into the sarcoplasmic reticulum. Using magic angle spinning NMR, we monitored the chemical shifts of the methylene and methyl groups of the derivatized cysteine residues along the major steps of the enzymatic cycle. The methylene chemical shifts are sensitive to the ATPase conformational changes induced upon nucleotide and Ca(2+) ion binding and are ideal probes for active and inactive states of the enzyme. This new approach is extendable to large mammalian enzymes and signaling proteins with native or engineered cysteine residues in their amino acid sequence.",
keywords = "Animals, Binding Sites, Calcium/metabolism, Cysteine/analysis, Lipid Bilayers/chemistry, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Rabbits, Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry",
author = "Vostrikov, {Vitaly V} and Martin Gustavsson and Tata Gopinath and Dan Mullen and Dicke, {Alysha A} and Vincent Truong and Gianluigi Veglia",
year = "2016",
month = feb,
day = "19",
doi = "10.1021/acschembio.5b00953",
language = "English",
volume = "11",
pages = "329--34",
journal = "A C S Chemical Biology",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "2",

}

RIS

TY - JOUR

T1 - Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR

AU - Vostrikov, Vitaly V

AU - Gustavsson, Martin

AU - Gopinath, Tata

AU - Mullen, Dan

AU - Dicke, Alysha A

AU - Truong, Vincent

AU - Veglia, Gianluigi

PY - 2016/2/19

Y1 - 2016/2/19

N2 - To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by NMR at atomic resolution has been challenging due to the large size of these systems. It is further exacerbated for large mammalian proteins that are difficult to express and label with NMR-active isotopes. Here, we synthesized and engineered (13)C ethyl groups on native cysteines to map the structural transitions of the sarcoplasmic reticulum Ca(2+)-ATPase, a 110 kDa transmembrane enzyme that transports Ca(2+) into the sarcoplasmic reticulum. Using magic angle spinning NMR, we monitored the chemical shifts of the methylene and methyl groups of the derivatized cysteine residues along the major steps of the enzymatic cycle. The methylene chemical shifts are sensitive to the ATPase conformational changes induced upon nucleotide and Ca(2+) ion binding and are ideal probes for active and inactive states of the enzyme. This new approach is extendable to large mammalian enzymes and signaling proteins with native or engineered cysteine residues in their amino acid sequence.

AB - To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by NMR at atomic resolution has been challenging due to the large size of these systems. It is further exacerbated for large mammalian proteins that are difficult to express and label with NMR-active isotopes. Here, we synthesized and engineered (13)C ethyl groups on native cysteines to map the structural transitions of the sarcoplasmic reticulum Ca(2+)-ATPase, a 110 kDa transmembrane enzyme that transports Ca(2+) into the sarcoplasmic reticulum. Using magic angle spinning NMR, we monitored the chemical shifts of the methylene and methyl groups of the derivatized cysteine residues along the major steps of the enzymatic cycle. The methylene chemical shifts are sensitive to the ATPase conformational changes induced upon nucleotide and Ca(2+) ion binding and are ideal probes for active and inactive states of the enzyme. This new approach is extendable to large mammalian enzymes and signaling proteins with native or engineered cysteine residues in their amino acid sequence.

KW - Animals

KW - Binding Sites

KW - Calcium/metabolism

KW - Cysteine/analysis

KW - Lipid Bilayers/chemistry

KW - Models, Molecular

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Conformation

KW - Rabbits

KW - Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry

U2 - 10.1021/acschembio.5b00953

DO - 10.1021/acschembio.5b00953

M3 - Journal article

C2 - 26650884

VL - 11

SP - 329

EP - 334

JO - A C S Chemical Biology

JF - A C S Chemical Biology

SN - 1554-8929

IS - 2

ER -

ID: 329434811