PDBsum entry 4c0l

Hydrolase

PDB id: 4c0l

Contents

Protein chain

404 a.a.

Ligands

UNX

SO4 ×3

GDP

HSE

Metals

_NA

_MG ×2

Waters ×17

PDB id:

4c0l

Name:

Hydrolase

Title:

Crystal structure of drosophila miro ef hand and cgtpase domains bound to one magnesium ion and mg:gdp (mggdp-miros)

Structure:

Mitochondrial rho gtpase. Chain: a. Fragment: elm1, elm2, and cgtpase, residues 201-467. Synonym: miro, dmiro. Engineered: yes

Source:

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

Resolution:

3.00Å R-factor: 0.217 R-free: 0.259

Authors:

J.L.Klosowiak,P.J.Focia,Z.Wawrzak,S.Chakravarthy,E.C.Landahl, D.M.Freymann,S.E.Rice

Key ref:

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: 24071720 DOI: 10.1038/embor.2013.151

Date:

05-Aug-13 Release date: 09-Oct-13

Protein chain

Q8IMX7  (MIRO_DROME) -  Mitochondrial Rho GTPase from Drosophila melanogaster

Seq: 652 a.a.

Struc: 404 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.5.- - ?????

DOI no: 10.1038/embor.2013.151

Embo Rep 14:968-974 (2013)

PubMed id: 24071720

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

J.L.Klosowiak, P.J.Focia, S.Chakravarthy, E.C.Landahl, D.M.Freymann, S.E.Rice.

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.