View source for 4eag


==Co-crystal structure of an chimeric AMPK core with ATP==
<StructureSection load='4eag' size='340' side='right'caption='[[4eag]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.701&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [https://pdbe.org/4eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [https://www.ebi.ac.uk/pdbsum/4eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O18645_DROME O18645_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the gamma subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the gamma subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes.,Chen L, Wang J, Zhang YY, Yan SF, Neumann D, Schlattner U, Wang ZX, Wu JW Nat Struct Mol Biol. 2012 Jun 3;19(7):716-8. doi: 10.1038/nsmb.2319. PMID:22659875<ref>PMID:22659875</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4eag" style="background-color:#fffaf0;"></div>

==See Also==
*[[AMP-activated protein kinase 3D structures|AMP-activated protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Chen L]]
[[Category: Neumann D]]
[[Category: Schlattner U]]
[[Category: Wang J]]
[[Category: Wang Z-X]]
[[Category: Wu J-W]]
[[Category: Yan SF]]
[[Category: Zhang Y-Y]]