8jfk
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==PhK holoenzyme in inactive state, muscle isoform== | |
+ | <StructureSection load='8jfk' size='340' side='right'caption='[[8jfk]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8jfk]] is a 16 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=8JFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFK FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAR:FARNESYL'>FAR</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=8jfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfk OCA], [https://pdbe.org/8jfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfk RCSB], [https://www.ebi.ac.uk/pdbsum/8jfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfk ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/KPBB_HUMAN KPBB_HUMAN] Glycogen storage disease due to liver and muscle phosphorylase kinase deficiency. The disease is caused by variants affecting the gene represented in this entry. | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/KPBB_HUMAN KPBB_HUMAN] Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The study of phosphorylase kinase (PhK)-regulated glycogen metabolism has contributed to the fundamental understanding of protein phosphorylation; however, the molecular mechanism of PhK remains poorly understood. Here we present the high-resolution cryo-electron microscopy structures of human muscle PhK. The 1.3-megadalton PhK alpha(4)beta(4)gamma(4)delta(4) hexadecamer consists of a tetramer of tetramer, wherein four alphabetagammadelta modules are connected by the central beta(4) scaffold. The alpha- and beta-subunits possess glucoamylase-like domains, but exhibit no detectable enzyme activities. The alpha-subunit serves as a bridge between the beta-subunit and the gammadelta subcomplex, and facilitates the gamma-subunit to adopt an autoinhibited state. Ca(2+)-free calmodulin (delta-subunit) binds to the gamma-subunit in a compact conformation. Upon binding of Ca(2+), a conformational change occurs, allowing for the de-inhibition of the gamma-subunit through a spring-loaded mechanism. We also reveal an ADP-binding pocket in the beta-subunit, which plays a role in allosterically enhancing PhK activity. These results provide molecular insights of this important kinase complex. | ||
- | + | Architecture and activation of human muscle phosphorylase kinase.,Yang X, Zhu M, Lu X, Wang Y, Xiao J Nat Commun. 2024 Mar 28;15(1):2719. doi: 10.1038/s41467-024-47049-2. PMID:38548794<ref>PMID:38548794</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 8jfk" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Xiao JY]] | ||
+ | [[Category: Yang XK]] |
Current revision
PhK holoenzyme in inactive state, muscle isoform
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