ArticleThe Journal of biological chemistry2014
Evidence supporting the 19 β-strand model for Tom40 from cysteine scanning and protease site accessibility studies.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import.Advances in experimental medicine and biology · 2026Review
- Role of the Mitochondrial Protein Import Machinery and Protein Processing in Heart Disease.Frontiers in cardiovascular medicine · 2021Review
- Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.Nature structural & molecular biology · 2019Article
- Translocase of the Outer Mitochondrial Membrane 40 Is Required for Mitochondrial Biogenesis and Embryo Development inFrontiers in plant science · 2019Article
- Structural characterisation of a full-length mitochondrial outer membrane TOM40 preprotein translocase: implications for its interaction with presequence peptides.European biophysics journal : EBJ · 2019Article
- Ten Years of High Resolution Structural Research on the Voltage Dependent Anion Channel (VDAC)-Recent Developments and Future Directions.Frontiers in physiology · 2018Review
- Cell biology: Architecture of a protein entry gate.Nature · 2015Article
- Dual mechanism of ion permeation through VDAC revealed with inorganic phosphate ions and phosphate metabolites.PloS one · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Most proteins found in mitochondria are translated in the cytosol and enter the organelle via the TOM complex (translocase of the outer mitochondrial membrane). Tom40 is the pore forming component of the complex. Although the three-dimensional structure of Tom40 has not been determined, the structure of porin, a related protein, has been shown to be a β-barrel containing 19 membrane spanning β-strands and an N-terminal α-helical region. The evolutionary relationship between the two proteins has allowed modeling of Tom40 into a similar structure by several laboratories. However, it has been suggested that the 19-strand porin structure does not represent the native form of the protein. If true, modeling of Tom40 based on the porin structure would also be invalid. We have used substituted cysteine accessibility mapping to identify several potential β-strands in the Tom40 protein in isolated mitochondria. These data, together with protease accessibility studies, support the 19 β-strand model for Tom40 with the C-terminal end of the protein localized to the intermembrane space.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.