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-Structure paper
Title | Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane. |
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Journal, issue, pages | J Cell Biol, Vol. 199, Issue 4, Page 599-611, Year 2012 |
Publish date | Nov 12, 2012 |
![]() | Astrid Klein / Lars Israel / Sebastian W K Lackey / Frank E Nargang / Axel Imhof / Wolfgang Baumeister / Walter Neupert / Dennis R Thomas / ![]() |
PubMed Abstract | The TOB-SAM complex is an essential component of the mitochondrial outer membrane that mediates the insertion of β-barrel precursor proteins into the membrane. We report here its isolation and ...The TOB-SAM complex is an essential component of the mitochondrial outer membrane that mediates the insertion of β-barrel precursor proteins into the membrane. We report here its isolation and determine its size, composition, and structural organization. The complex from Neurospora crassa was composed of Tob55-Sam50, Tob38-Sam35, and Tob37-Sam37 in a stoichiometry of 1:1:1 and had a molecular mass of 140 kD. A very minor fraction of the purified complex was associated with one Mdm10 protein. Using molecular homology modeling for Tob55 and cryoelectron microscopy reconstructions of the TOB complex, we present a model of the TOB-SAM complex that integrates biochemical and structural data. We discuss our results and the structural model in the context of a possible mechanism of the TOB insertase. |
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Methods | EM (single particle) |
Resolution | 13.4 - 15.6 Å |
Structure data | ![]() EMDB-2195: ![]() EMDB-2196: ![]() EMDB-2197: ![]() EMDB-2200: ![]() EMDB-2201: ![]() EMDB-2202: ![]() EMDB-2203: |
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