Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.0
Classification:HYDROLASE
Release Date:2013-10-09
Deposition Date:2013-08-05
Revision Date:2013-11-13
Molecular Weight:50040.64
Macromolecule Type:Protein
Residue Count:423
Atom Site Count:3300
DOI:10.2210/pdb4c0l/pdb
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.
Resolution:3.0
Classification:HYDROLASE
Release Date:2013-10-09
Deposition Date:2013-08-05
Revision Date:2013-11-13
Molecular Weight:50040.64
Macromolecule Type:Protein
Residue Count:423
Atom Site Count:3300
DOI:10.2210/pdb4c0l/pdb
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.
| Date made available | 2013 |
|---|---|
| Publisher | RCSB-PDB |