2qlv

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[[Image:2qlv.jpg|left|200px]]
 
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==Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1==
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The line below this paragraph, containing "STRUCTURE_2qlv", creates the "Structure Box" on the page.
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<StructureSection load='2qlv' size='340' side='right'caption='[[2qlv]], [[Resolution|resolution]] 2.60&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'>[[2qlv]] is a 6 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=2QLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QLV 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]] 2.6&#8491;</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=2qlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qlv OCA], [https://pdbe.org/2qlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qlv RCSB], [https://www.ebi.ac.uk/pdbsum/2qlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qlv ProSAT]</span></td></tr>
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{{STRUCTURE_2qlv| PDB=2qlv | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1'''
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[https://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals and is an attractive target for drug discovery against diabetes, obesity and other diseases. The AMPK homologue in Saccharomyces cerevisiae, known as SNF1, is essential for responses to glucose starvation as well as for other cellular processes, although SNF1 seems to be activated by a ligand other than AMP. Here we report the crystal structure at 2.6 A resolution of the heterotrimer core of SNF1. The ligand-binding site in the gamma-subunit (Snf4) has clear structural differences from that of the Schizosaccharomyces pombe enzyme, although our crystallographic data indicate that AMP can also bind to Snf4. The glycogen-binding domain in the beta-subunit (Sip2) interacts with Snf4 in the heterotrimer but should still be able to bind carbohydrates. Our structure is supported by a large body of biochemical and genetic data on this complex. Most significantly, the structure reveals that part of the regulatory sequence in the alpha-subunit (Snf1) is sequestered by Snf4, demonstrating a direct interaction between the alpha- and gamma-subunits and indicating that our structure may represent the heterotrimer core of SNF1 in its activated state.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ql/2qlv_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2QLV is a [[Protein complex]] structure of sequences 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=2QLV OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2qlv ConSurf].
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Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1., Amodeo GA, Rudolph MJ, Tong L, Nature. 2007 Sep 27;449(7161):492-5. Epub 2007 Sep 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17851534 17851534]
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<div style="clear:both"></div>
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[[Category: Non-specific serine/threonine protein kinase]]
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== References ==
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[[Category: Protein complex]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Amodeo, G A.]]
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[[Category: Amodeo GA]]
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[[Category: Rudolph, M J.]]
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[[Category: Rudolph MJ]]
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[[Category: Tong, L.]]
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[[Category: Tong L]]
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[[Category: Atp-binding]]
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[[Category: Carbohydrate metabolism]]
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[[Category: Cbs domain]]
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[[Category: Heterotrimer]]
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[[Category: Kinase]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Myristate]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphorylation]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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[[Category: Transferase/protein binding complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:10:36 2008''
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Current revision

Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1

PDB ID 2qlv

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