View source for 8jfk


==PhK holoenzyme in inactive state, muscle isoform==
<StructureSection load='8jfk' size='340' side='right'caption='[[8jfk]], [[Resolution|resolution]] 2.90&Aring;' 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]] 2.9&#8491;</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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]]