4C0J

Crystal structure of Drosophila Miro EF hand and cGTPase domains in the apo state (Apo-MiroS)

Summary for 4C0J

• Entry DOI: 10.2210/pdb4c0j/pdb
• Related: 4C0K 4C0L
• Descriptor: MITOCHONDRIAL RHO GTPASE, UNKNOWN ATOM OR ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, mitochondrial transport, calcium-binding gtpase, kinesin, mitophagy, hidden ef hands
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Cellular location: Mitochondrion outer membrane; Single-pass type IV membrane protein (Probable): Q8IMX7
• Total number of polymer chains: 1
• Total formula weight: 49644.89

Authors

Klosowiak, J.L.,Focia, P.J.,Wawrzak, Z.,Chakravarthy, S.,Landahl, E.C.,Freymann, D.M.,Rice, S.E. (deposition date: 2013-08-05, release date: 2013-10-09, Last modification date: 2024-05-01)

Primary citation

Klosowiak, J.L.,Focia, P.J.,Chakravarthy, S.,Landahl, E.C.,Freymann, D.M.,Rice, S.E.
Structural Coupling of the EF Hand and C-Terminal Gtpase Domains in the Mitochondrial Protein Miro.
Embo Rep., 14:968-, 2013

PubMed Abstract: 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.

PubMed: 24071720
DOI: 10.1038/EMBOR.2013.151

Experimental method

X-RAY DIFFRACTION (2.82 Å)