View source for 5kty


==hMiro EF hand and cGTPase domains, GDP and Ca2+ bound state==
<StructureSection load='5kty' size='340' side='right'caption='[[5kty]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kty]] 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=5KTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTY 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]] 2.522&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5kty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kty OCA], [https://pdbe.org/5kty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kty RCSB], [https://www.ebi.ac.uk/pdbsum/5kty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kty ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MIRO1_HUMAN MIRO1_HUMAN] Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.<ref>PMID:12482879</ref> <ref>PMID:16630562</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hereditary Parkinson's disease is commonly caused by mutations in the protein kinase PINK1 or the E3 ubiquitin ligase Parkin, which function together to eliminate damaged mitochondria. PINK1 phosphorylates both Parkin and ubiquitin to stimulate ubiquitination of dozens of proteins on the surface of the outer mitochondrial membrane. However, the mechanisms by which Parkin recognizes specific proteins for modification remain largely unexplored. Here, we show that the C-terminal GTPase (cGTPase) of the Parkin primary substrate human Miro is necessary and sufficient for efficient ubiquitination. We present several new X-ray crystal structures of both human Miro1 and Miro2 that reveal substrate recognition and ubiquitin transfer to be specific to particular protein domains and lysine residues. We also provide evidence that Parkin substrate recognition is functionally separate from substrate modification. Finally, we show that prioritization for modification of a specific lysine sidechain of the cGTPase (K572) within human Miro1 is dependent on both its location and chemical microenvironment. Activation of Parkin by phosphorylation or by binding of pUb is required for prioritization of K572 for modification, suggesting that Parkin activation and acquisition of substrate specificity are coupled.

Structural insights into Parkin substrate lysine targeting from minimal Miro substrates.,Klosowiak JL, Park S, Smith KP, French ME, Focia PJ, Freymann DM, Rice SE Sci Rep. 2016 Sep 8;6:33019. doi: 10.1038/srep33019. PMID:27605430<ref>PMID:27605430</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kty" style="background-color:#fffaf0;"></div>

==See Also==
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Focia PJ]]
[[Category: Freymann DM]]
[[Category: Klosowiak JL]]
[[Category: Rice SE]]