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PDBsum entry 4c0j
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PDB id:
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Hydrolase
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Title:
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Crystal structure of drosophila miro ef hand and cgtpase domains in the apo state (apo-miros)
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Structure:
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Mitochondrial rho gtpase. Chain: a. Fragment: elm1, elm2, and cgtpase, residues 201-617. Synonym: miro, dmiro. Engineered: yes. Other_details: drosophila miro residues 201-617
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Source:
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Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codonplus rp. Other_details: drosophila genomics resource center clone re22983
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Resolution:
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2.82Å
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R-factor:
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0.229
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R-free:
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0.262
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Authors:
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J.L.Klosowiak,P.J.Focia,Z.Wawrzak,S.Chakravarthy,E.C.Landahl, D.M.Freymann,S.E.Rice
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Key ref:
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J.L.Klosowiak
et al.
(2013).
Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro.
Embo Rep,
14,
968-974.
PubMed id:
DOI:
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Date:
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05-Aug-13
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Release date:
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09-Oct-13
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PROCHECK
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Headers
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References
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Q8IMX7
(MIRO_DROME) -
Mitochondrial Rho GTPase from Drosophila melanogaster
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Seq:
Struc:
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652 a.a.
404 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Embo Rep
14:968-974
(2013)
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PubMed id:
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Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro.
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J.L.Klosowiak,
P.J.Focia,
S.Chakravarthy,
E.C.Landahl,
D.M.Freymann,
S.E.Rice.
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ABSTRACT
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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.
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