Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro.

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.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Klosowiak JL,Focia PJ,Chakravarthy S,Landahl EC,Freymann DM,Rice SE

doi

10.1038/embor.2013.151

subject

Has Abstract

pub_date

2013-11-01 00:00:00

pages

968-74

issue

11

eissn

1469-221X

issn

1469-3178

pii

embor2013151

journal_volume

14

pub_type

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