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-Structure paper
タイトル | Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. |
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ジャーナル・号・ページ | Cell, Vol. 170, Issue 4, Page 693-700.e7, Year 2017 |
掲載日 | 2017年8月10日 |
著者 | Thomas Bausewein / Deryck J Mills / Julian D Langer / Beate Nitschke / Stephan Nussberger / Werner Kühlbrandt / |
PubMed 要旨 | The TOM complex is the main entry gate for protein precursors from the cytosol into mitochondria. We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM). The ...The TOM complex is the main entry gate for protein precursors from the cytosol into mitochondria. We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM). The complex is a 148 kDa symmetrical dimer of ten membrane protein subunits that create a shallow funnel on the cytoplasmic membrane surface. In the core of the dimer, the β-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the α-helical subunits Tom5, Tom6, and Tom7. Tom22, the central preprotein receptor, connects the two Tom40 pores at the dimer interface. Our structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery. |
リンク | Cell / PubMed:28802041 |
手法 | EM (単粒子) |
解像度 | 6.8 Å |
構造データ | |
由来 |
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キーワード | PROTEIN TRANSPORT / TOM-Complex / Protein Import / Mitochondria / Cryo-EM |