Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis

Polekhina, Galina; Feil, Susanne C.; Gupta, Abhilasha; O’Donnell, Paul; Stapleton, David; Parker, Michael W.

doi:10.1107/S1744309104025059

Title: Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis

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Abstract

The glycogen-binding domain of the AMP-activated kinase β subunit has been crystallized in the presence of β-cyclodextrin. The structure has been determined by single isomorphous replacement and threefold averaging using in-house X-ray data collected from selenomethionine-substituted protein. AMP-activated protein kinase (AMPK) is an intracellular energy sensor that regulates metabolism in response to energy demand and supply by adjusting the ATP-generating and ATP-consuming pathways. AMPK potentially plays a critical role in diabetes and obesity as it is known to be activated by metforin and rosiglitazone, drugs used for the treatment of type II diabetes. AMPK is a heterotrimer composed of a catalytic α subunit and two regulatory subunits, β and γ. Mutations in the γ subunit are known to cause glycogen accumulation, leading to cardiac arrhythmias. Recently, a functional glycogen-binding domain (GBD) has been identified in the β subunit. Here, the crystallization of GBD in the presence of β-cyclodextrin is reported together with preliminary X-ray data analysis allowing the determination of the structure by single isomorphous replacement and threefold averaging using in-house X-ray data collected from a selenomethionine-substituted protein.

Authors:

Polekhina, Galina; Feil, Susanne C.; Gupta, Abhilasha ^[1]; O’Donnell, Paul ^[2]; Stapleton, David; Parker, Michael W. ^[1]

St Vincent’s Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065 (Australia)
Department of Biochemistry and Molecular Biology, The University of Melbourne, Parkville 3010 (Australia)

Publication Date:: Sat Jan 01 00:00:00 EST 2005

OSTI Identifier:: 22356070

Resource Type:: Journal Article

Journal Name:: Acta Crystallographica. Section F

Additional Journal Information:: Journal Volume: 61; Journal Issue: Pt 1; Other Information: PMCID: PMC1952378; PMID: 16508085; PUBLISHER-ID: en5061; OAI: oai:pubmedcentral.nih.gov:1952378; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091

Country of Publication:: United Kingdom

Language:: English

Subject:: 46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BUILDUP; CRYSTALLIZATION; DATA ANALYSIS; SENSORS

Citation Formats


                    Polekhina, Galina, Feil, Susanne C., Gupta, Abhilasha, O’Donnell, Paul, Stapleton, David, and Parker, Michael W. Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis.  United Kingdom: N. p., 2005. 
        Web.  doi:10.1107/S1744309104025059.

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                    Polekhina, Galina, Feil, Susanne C., Gupta, Abhilasha, O’Donnell, Paul, Stapleton, David, & Parker, Michael W. Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis.  United Kingdom.  https://doi.org/10.1107/S1744309104025059

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                    Polekhina, Galina, Feil, Susanne C., Gupta, Abhilasha, O’Donnell, Paul, Stapleton, David, and Parker, Michael W. 2005.  
        "Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis".  United Kingdom.  https://doi.org/10.1107/S1744309104025059.

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@article{osti_22356070,

  title        = {Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis},

  author       = {Polekhina, Galina and Feil, Susanne C. and Gupta, Abhilasha and O’Donnell, Paul and Stapleton, David and Parker, Michael W.},

  abstractNote = {The glycogen-binding domain of the AMP-activated kinase β subunit has been crystallized in the presence of β-cyclodextrin. The structure has been determined by single isomorphous replacement and threefold averaging using in-house X-ray data collected from selenomethionine-substituted protein. AMP-activated protein kinase (AMPK) is an intracellular energy sensor that regulates metabolism in response to energy demand and supply by adjusting the ATP-generating and ATP-consuming pathways. AMPK potentially plays a critical role in diabetes and obesity as it is known to be activated by metforin and rosiglitazone, drugs used for the treatment of type II diabetes. AMPK is a heterotrimer composed of a catalytic α subunit and two regulatory subunits, β and γ. Mutations in the γ subunit are known to cause glycogen accumulation, leading to cardiac arrhythmias. Recently, a functional glycogen-binding domain (GBD) has been identified in the β subunit. Here, the crystallization of GBD in the presence of β-cyclodextrin is reported together with preliminary X-ray data analysis allowing the determination of the structure by single isomorphous replacement and threefold averaging using in-house X-ray data collected from a selenomethionine-substituted protein.},

  doi          = {10.1107/S1744309104025059},

  url          = {https://www.osti.gov/biblio/22356070},
  journal      = {Acta Crystallographica. Section F},

  issn         = {1744-3091},

  number       = Pt 1,

  volume       = 61,

  place        = {United Kingdom},

  year         = {Sat Jan 01 00:00:00 EST 2005},

  month        = {Sat Jan 01 00:00:00 EST 2005}

}

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