3jrw

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{{Seed}}
 
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[[Image:3jrw.jpg|left|200px]]
 
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==Phosphorylated BC domain of ACC2==
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The line below this paragraph, containing "STRUCTURE_3jrw", creates the "Structure Box" on the page.
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<StructureSection load='3jrw' size='340' side='right'caption='[[3jrw]], [[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'>[[3jrw]] 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=3JRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JRW 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]] 2.6&#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=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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{{STRUCTURE_3jrw| PDB=3jrw | 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=3jrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jrw OCA], [https://pdbe.org/3jrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jrw RCSB], [https://www.ebi.ac.uk/pdbsum/3jrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jrw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACACB_HUMAN ACACB_HUMAN] ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
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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/jr/3jrw_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=3jrw 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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Acetyl-CoA carboxylases (ACCs) have been highlighted as therapeutic targets for obesity and diabetes, as they play crucial roles in fatty acid metabolism. ACC activity is regulated through the short-term mechanism of inactivation by reversible phosphorylation. Here, we report the crystal structures of the biotin carboxylase (BC) domain of human ACC2 phosphorylated by AMP-activated protein kinase (AMPK). The phosphorylated Ser222 binds to the putative dimer interface of BC, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. We also determined the structure of the human BC domain in complex with soraphen A, a macrocyclic polyketide natural product. This structure shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK.
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===Phosphorylated BC domain of ACC2===
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Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK.,Cho YS, Lee JI, Shin D, Kim HT, Jung HY, Lee TG, Kang LW, Ahn YJ, Cho HS, Heo YS Biochem Biophys Res Commun. 2010 Jan 1;391(1):187-92. Epub 2009 Nov 10. PMID:19900410<ref>PMID:19900410</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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<div class="pdbe-citations 3jrw" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19900410}}, adds the Publication Abstract to the page
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*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19900410 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19900410}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3JRW is a 1 chain structure of 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=3JRW OCA].
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==Reference==
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<ref group="xtra">PMID:19900410</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Cho, Y S.]]
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[[Category: Large Structures]]
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[[Category: Heo, Y S.]]
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[[Category: Cho YS]]
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[[Category: Kim, H T.]]
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[[Category: Heo YS]]
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[[Category: Lee, J I.]]
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[[Category: Kim HT]]
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[[Category: Lee, T G.]]
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[[Category: Lee JI]]
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[[Category: Shin, D.]]
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[[Category: Lee TG]]
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[[Category: Alternative splicing]]
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[[Category: Shin D]]
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[[Category: Atp-binding]]
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[[Category: Bc domain]]
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[[Category: Biotin]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Ligase]]
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[[Category: Lipid synthesis]]
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[[Category: Manganese]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Multifunctional enzyme]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 14:04:04 2010''
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Current revision

Phosphorylated BC domain of ACC2

PDB ID 3jrw

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