View source for 6djx


==Crystal Structure of pParkin-pUb-UbcH7 complex==
<StructureSection load='6djx' size='340' side='right'caption='[[6djx]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6djx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bactrocera_dorsalis Bactrocera dorsalis], [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DJX 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]] 4.801&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6djx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6djx OCA], [https://pdbe.org/6djx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6djx RCSB], [https://www.ebi.ac.uk/pdbsum/6djx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6djx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A034W4L8_BACDO A0A034W4L8_BACDO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutations in the ubiquitin ligase parkin are responsible for a familial form of Parkinson's disease. Parkin and the PINK1 kinase regulate a quality-control system for mitochondria. PINK1 phosphorylates ubiquitin on the outer membrane of damaged mitochondria, thus leading to recruitment and activation of parkin via phosphorylation of its ubiquitin-like (Ubl) domain. Here, we describe the mechanism of parkin activation by phosphorylation. The crystal structure of phosphorylated Bactrocera dorsalis (oriental fruit fly) parkin in complex with phosphorylated ubiquitin and an E2 ubiquitin-conjugating enzyme reveals that the key activating step is movement of the Ubl domain and release of the catalytic RING2 domain. Hydrogen/deuterium exchange and NMR experiments with the various intermediates in the activation pathway confirm and extend the interpretation of the crystal structure to mammalian parkin. Our results rationalize previously unexplained Parkinson's disease mutations and the presence of internal linkers that allow large domain movements in parkin.

Mechanism of parkin activation by phosphorylation.,Sauve V, Sung G, Soya N, Kozlov G, Blaimschein N, Miotto LS, Trempe JF, Lukacs GL, Gehring K Nat Struct Mol Biol. 2018 Jul;25(7):623-630. doi: 10.1038/s41594-018-0088-7. Epub, 2018 Jul 2. PMID:29967542<ref>PMID:29967542</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6djx" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bactrocera dorsalis]]
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gehring K]]
[[Category: Sauve V]]
[[Category: Sung G]]
[[Category: Trempe JF]]