2uv5

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==CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP==
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<StructureSection load='2uv5' size='340' side='right' caption='[[2uv5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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==Crystal Structure of a CBS domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP==
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<StructureSection load='2uv5' size='340' side='right'caption='[[2uv5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2uv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UV5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2uv5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UV5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMZ:AMINOIMIDAZOLE+4-CARBOXAMIDE+RIBONUCLEOTIDE'>AMZ</scene></td></tr>
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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]] 1.69&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2uv4|2uv4]], [[2uv6|2uv6]], [[2uv7|2uv7]]</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=AMZ:AMINOIMIDAZOLE+4-CARBOXAMIDE+RIBONUCLEOTIDE'>AMZ</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uv5 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv5 PDBsum]</span></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=2uv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv5 OCA], [https://pdbe.org/2uv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uv5 RCSB], [https://www.ebi.ac.uk/pdbsum/2uv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uv5 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAKG1_HUMAN AAKG1_HUMAN] AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:21680840</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uv/2uv5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uv/2uv5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2uv5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2uv5" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[AMP-activated protein kinase|AMP-activated protein kinase]]
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*[[AMP-activated protein kinase 3D structures|AMP-activated protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Cleasby, A]]
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[[Category: Large Structures]]
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[[Category: Day, P]]
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[[Category: Cleasby A]]
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[[Category: Horer, S]]
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[[Category: Day P]]
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[[Category: Nar, H]]
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[[Category: Horer S]]
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[[Category: Parra, L]]
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[[Category: Nar H]]
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[[Category: Redemann, N]]
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[[Category: Parra L]]
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[[Category: Sharff, A]]
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[[Category: Redemann N]]
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[[Category: Tickle, I]]
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[[Category: Sharff A]]
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[[Category: Williams, M]]
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[[Category: Tickle I]]
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[[Category: Yon, J]]
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[[Category: Williams M]]
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[[Category: Ampk gamma1 subunit cbs 3 plus 4 amp regulatory subunit some]]
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[[Category: Yon J]]
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[[Category: Cbs domain]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of a CBS domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP

PDB ID 2uv5

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