5o8o
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TOM40_NEUCR TOM40_NEUCR]] Channel-forming protein essential for import of protein precursors into mitochondria.<ref>PMID:11402060</ref> | [[http://www.uniprot.org/uniprot/TOM40_NEUCR TOM40_NEUCR]] Channel-forming protein essential for import of protein precursors into mitochondria.<ref>PMID:11402060</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 beta-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the alpha-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. | ||
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| + | Cryo-EM Structure of the TOM Core Complex from Neurospora crassa.,Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, Kuhlbrandt W Cell. 2017 Aug 10;170(4):693-700.e7. doi: 10.1016/j.cell.2017.07.012. PMID:28802041<ref>PMID:28802041</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5o8o" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:33, 24 October 2018
N. crassa Tom40 model based on cryo-EM structure of the TOM core complex at 6.8 A
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