5kso

hMiro1 C-domain GDP-Pi Complex P3121 Crystal Form

spinqualitylabelsall models 5kso, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kso is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, PO4 Related: 5ksp, 5ksy, 5ksz, 5kty, 5ku1, 5kut Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MIRO1_HUMAN] Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Rho GTPase

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