Structural coupling of the EF hand and C‐terminal GTPase domains in the mitochondrial protein Miro
| Autor: | Srinivas Chakravarthy, Pamela J. Focia, Sarah E. Rice, Eric C. Landahl, Douglas M. Freymann, Julian L. Klosowiak |
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| Rok vydání: | 2013 |
| Předmět: |
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Molecular rho GTP-Binding Proteins Ubiquitin-Protein Ligases Molecular Sequence Data PINK1 GTPase Biology Mitochondrion Ligands Biochemistry Mitochondrial Proteins Genetics Animals Drosophila Proteins Amino Acid Sequence EF Hand Motifs Molecular Biology Peptide sequence Mitochondrial transport EF hand Scientific Reports Ubiquitination Protein Structure Tertiary Cell biology Solutions Drosophila melanogaster ras Proteins Drosophila Protein Alpha helix |
| Zdroj: | EMBO reports. 14:968-974 |
| ISSN: | 1469-3178 1469-221X |
| Popis: | Miro is a highly conserved calcium-binding GTPase at the regulatory nexus of mitochondrial transport and autophagy. Here we present crystal structures comprising the tandem EF hand and carboxy terminal GTPase (cGTPase) domains of Drosophila Miro. The structures reveal two previously unidentified 'hidden' EF hands, each paired with a canonical EF hand. Each EF hand pair is bound to a helix that structurally mimics an EF hand ligand. A key nucleotide-sensing element and a Pink1 phosphorylation site both lie within an extensive EF hand-cGTPase interface. Our results indicate structural mechanisms for calcium, nucleotide and phosphorylation-dependent regulation of mitochondrial function by Miro. |
| Databáze: | OpenAIRE |
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