2nye

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{{Seed}}
 
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[[Image:2nye.png|left|200px]]
 
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==Crystal structure of the Bateman2 domain of yeast Snf4==
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The line below this paragraph, containing "STRUCTURE_2nye", creates the "Structure Box" on the page.
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<StructureSection load='2nye' size='340' side='right'caption='[[2nye]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2nye]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NYE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2nye| PDB=2nye | SCENE= }}
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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=2nye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nye OCA], [https://pdbe.org/2nye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nye RCSB], [https://www.ebi.ac.uk/pdbsum/2nye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nye ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAKG_YEAST AAKG_YEAST] Adenine nucleotides-binding subunit gamma 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. 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 (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:10099331</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:1468623</ref> <ref>PMID:18474591</ref> <ref>PMID:2169717</ref> <ref>PMID:22019086</ref> <ref>PMID:2557546</ref> <ref>PMID:3049551</ref> <ref>PMID:3939253</ref> <ref>PMID:6392017</ref> <ref>PMID:7050076</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:9600950</ref>
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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/ny/2nye_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2nye ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. AMP is believed to control the activity of AMPK by binding to the gamma subunit of this heterotrimeric enzyme. This subunit contains two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. No structural information is currently available on this subunit, and the molecular basis for its interactions with AMP is not well understood. We report here the crystal structure at 1.9 Angstrom resolution of the Bateman2 domain of Snf4, the gamma subunit of the yeast ortholog of AMPK. The structure revealed a dimer of the Bateman2 domain, and this dimerization is supported by our light-scattering, mutagenesis, and biochemical studies. There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket.
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===Crystal structure of the Bateman2 domain of yeast Snf4===
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Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding.,Rudolph MJ, Amodeo GA, Iram SH, Hong SP, Pirino G, Carlson M, Tong L Structure. 2007 Jan;15(1):65-74. PMID:17223533<ref>PMID:17223533</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17223533}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2nye" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17223533 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17223533}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2NYE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYE OCA].
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==Reference==
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Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding., Rudolph MJ, Amodeo GA, Iram SH, Hong SP, Pirino G, Carlson M, Tong L, Structure. 2007 Jan;15(1):65-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17223533 17223533]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Amodeo GA]]
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[[Category: Amodeo, G A.]]
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[[Category: Carlson M]]
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[[Category: Carlson, M.]]
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[[Category: Hong S]]
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[[Category: Hong, S.]]
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[[Category: Iram S]]
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[[Category: Iram, S.]]
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[[Category: Pirino G]]
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[[Category: Pirino, G.]]
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[[Category: Rudolph MJ]]
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[[Category: Rudolph, M J.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: Amp kinase]]
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[[Category: Bateman2 domain]]
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[[Category: Snf4]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:20:59 2008''
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Current revision

Crystal structure of the Bateman2 domain of yeast Snf4

PDB ID 2nye

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