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1z0m

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(New page: 200px<br /><applet load="1z0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0m, resolution 1.910&Aring;" /> '''the glycogen-bindin...)
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[[Image:1z0m.gif|left|200px]]<br /><applet load="1z0m" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z0m, resolution 1.910&Aring;" />
 
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'''the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit'''<br />
 
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==Overview==
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==the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit==
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AMP-activated protein kinase (AMPK) coordinates cellular metabolism in, response to energy demand as well as to a variety of stimuli. The AMPK, beta subunit acts as a scaffold for the alpha catalytic and gamma, regulatory subunits and targets the AMPK heterotrimer to glycogen. We have, determined the structure of the AMPK beta glycogen binding domain in, complex with beta-cyclodextrin. The structure reveals a carbohydrate, binding pocket that consolidates all known aspects of carbohydrate binding, observed in starch binding domains into one site, with extensive contact, between several residues and five glucose units. beta-cyclodextrin is held, in a pincer-like grasp with two tryptophan residues cradling two, beta-cyclodextrin glucose units and a leucine residue piercing the, beta-cyclodextrin ring. Mutation of key beta-cyclodextrin binding residues, either partially or completely prevents the glycogen binding domain from, binding glycogen. Modeling suggests that this binding pocket enables AMPK, to interact with glycogen anywhere across the carbohydrate's helical, surface.
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<StructureSection load='1z0m' size='340' side='right'caption='[[1z0m]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z0m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0M FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900012:beta-cyclodextrin'>PRD_900012</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0m OCA], [https://pdbe.org/1z0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0m RCSB], [https://www.ebi.ac.uk/pdbsum/1z0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAKB1_RAT AAKB1_RAT] Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z0/1z0m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z0m ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1Z0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with BCD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z0M OCA].
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*[[AMP-activated protein kinase 3D structures|AMP-activated protein kinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for glycogen recognition by AMP-activated protein kinase., Polekhina G, Gupta A, van Denderen BJ, Feil SC, Kemp BE, Stapleton D, Parker MW, Structure. 2005 Oct;13(10):1453-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16216577 16216577]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Feil SC]]
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[[Category: Denderen, B.J.van.]]
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[[Category: Gupta A]]
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[[Category: Feil, S.C.]]
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[[Category: Kemp BE]]
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[[Category: Gupta, A.]]
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[[Category: Parker MW]]
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[[Category: Kemp, B.E.]]
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[[Category: Polekhina G]]
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[[Category: Parker, M.W.]]
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[[Category: Stapleton D]]
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[[Category: Polekhina, G.]]
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[[Category: Van Denderen BJ]]
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[[Category: Stapleton, D.]]
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[[Category: BCD]]
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[[Category: beta sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:10:18 2007''
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Current revision

the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit

PDB ID 1z0m

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